of an axoneme Image Chlamydomonas TEM 17.jpg thumb Micrograph of thin x section cut through Chlamydomonas axoneme Image IFTsimplified.JPG thumb A simplified model of intraflagellar transport. Numerous ... core consists of a cytoskeleton cytoskeletal structure called the axoneme . ref Cite pmid 11086017 ref The axoneme serves as the skeleton of these organelles , both giving support to the structure ... between cilia and flagella, the internal structure of the axoneme is common to both. Structure Inside cilia and flagella is a microtubule based cytoskeleton called the axoneme. The axoneme of primary cilia typically has a ring of nine outer microtubule doublets called a 9 0 axoneme , and the axoneme ... a 9 2 axoneme . The axonemal cytoskeleton acts as a scaffolding for various protein complexes and provides ... of the axoneme is the microtubule each axoneme is composed of several microtubules aligned in Parallel .... Besides the microtubules, the axoneme contains many protein s and protein complexes necessary ... out in a synchronized fashion, with the microtubules on one side of the axoneme being pulled down and those on the other side pulled up, the axoneme as a whole can bend back and forth. This process ... spoke is another protein complex of the axoneme. Thought to be important in regulating the motion of the axoneme, this T shaped complex projects from each set of outer doublets toward the central ... nexin linkages . Non motile primary cilia The axoneme structure in non motile primary cilia shows ..., and there is no pair of central microtubule singlets. This organization of axoneme is referred ... cite journal title The 9 2 Axoneme Anchors Multiple Inner Arm Dyneins and a Network of Kinases ... cite journal title An Integrative Model of Internal Axoneme Mechanics and External Fluid Dynamics ... more details
Orphan date April 2012 File Eukaryotic flagellum.svg thumb 200px Nexin can be located on this cross section of an axoneme Nexin is a proteinous inter doublet linkage that prevents microtubule s in the outer layer of axoneme s from movement with respect to each other. Otherwise vesicular transport protein s such as dynein would dissolve the whole structure. ref name boron26 cite book author Walter F., PhD. Boron title Medical Physiology A Cellular And Molecular Approach publisher Elsevier Saunders location year 2003 pages 1300 isbn 1 4160 2328 3 oclc doi Page 26 ref See also Sorting nexin References reflist Organelles Category Proteins fr nexine ... more details
about the structure within biological organisms the aspect of bicycle wheel design Bicycle wheel Lacing The radial spoke is a multi unit protein structure found in the axoneme s of eukaryotic cilia and flagella . ref name Karp2009 cite book author Gerald Karp title Cell and Molecular Biology Concepts and Experiments url http books.google.com books?id arRGYE0GxRQC&pg PA342 accessdate 25 November 2010 date 19 October 2009 publisher John Wiley and Sons isbn 9780470483374 pages 342 ref Although experiments have determined the importance of the radial spoke in the proper function of these organelle s, its structure and mode of action remain poorly understood. Cellular location and structure File Eukaryotic flagellum.svg thumb 250px The radial spoke shown in an axoneme cross section Radial spokes are T shaped structures present inside the axoneme. Each spoke consists of a head and a stalk, while each of these sub structures is itself made up of many protein subunits. ref name pmid16507594 cite journal author Yang P, Diener DR, Yang C, et al. title Radial spoke proteins of Chlamydomonas flagella journal J. Cell. Sci. volume 119 issue Pt 6 pages 1165 74 year 2006 month March pmid 16507594 pmc 1973137 doi 10.1242 jcs.02811 url http jcs.biologists.org cgi pmidlookup?view long&pmid 16507594 ref In all, the radial spoke is known to contain at least 17 different proteins, ref name pmid11402073 cite journal author Yang P, Diener DR, Rosenbaum JL, Sale WS title Localization of calmodulin and dynein light chain LC8 in flagellar radial spokes journal J. Cell Biol. volume 153 issue 6 pages 1315 26 year 2001 month June pmid 11402073 pmc 2192029 doi 10.1083 jcb.153.6.1315 url http www.jcb.org cgi pmidlookup?view long&pmid 11402073 ref with 5 located in the head and at least 12 making up the stalk. The spoke stalk binds to the A tubule of each microtubule outer doublet, and the spoke head faces in towards the center of the axoneme see illustration at right . Function The radial spoke is ... more details
More footnotes date April 2010 Image Axoneme cross section.svg thumb 280 Diagram of a cross section of the axoneme microtubule array present in all undulipodia. 1 A. and 1 B. Tubulin dimer units. 2. Central pair inside the central sheath. 3. Inner and outer arm of dynein . 4. Radial spoke. 5. Nexin . 6. Plasma membrane . File Eukaryotic flagellum.svg thumb left 200px Cross section of an axoneme An undulipodium or 9 2 organelle is an intracellular projection of a eukaryotic cell containing a microtubule array. Both eukaryotic flagella and eukaryotic cilia are considered undulipodia. ref name db2004 http www.encyclopedia.com doc 1O6 undulipodium.html A Dictionary of Biology , 2004, accessed 2010 04 06. ref This is a tertiary source, which is not the best source for Wikipedia per Wikipedia RS Primary.2C secondary.2C and tertiary sources however, I ve not yet been able to locate a secondary source to support this claim. N2e, 2010 04 06 Eukaryote Eukaryotic cilia are structurally identical to eukaryotic flagella, although distinctions are sometimes made according to function and or length. ref name Haimo JCB198112 cite journal author Haimo LT, Rosenbaum JL title Cilia, flagella, and microtubules journal J. Cell Biol. volume 91 issue 3 Pt 2 pages 125s 130s year 1981 month December pmid 6459327 doi 10.1083 jcb.91.3.125s url pmc 2112827 ref Flagella use a whip like action to create movement of the whole cell, such as the movement of spermatozoon sperm in the reproductive tract, and also create water movement as in the choanocyte s of sponge s. Citation needed date March 2010 Motile or secondary cilia are more numerous, with multiple cilia per cell, move in a wave like action, and are responsible for movement in organisms such as ciliates and Platyhelminthes , but also move extracellular substances in animals, such as the Respiratory epithelium Mucociliary Escalator ciliary escalator ... arrangement of microtubules known as an axoneme . At the base of the extension lies a structure called ... more details
Image Eukarya Flagella.svg thumb right Schematic of the eukaryotic flagellum. 1 axoneme, 2 cell membrane, 3 IFT Intraflagellar Transport , 4 Basal body, 5 Cross section of flagellum, 6 Triplets of microtubules of basal body. Image Chlamydomonas TEM 09.jpg thumb right Longitudinal section through the flagella area in Chlamydomonas reinhardtii . In the cell apex is the basal body that is the anchoring site for a flagellum. Basal bodies originate from and have a substructure similar to that of centrioles, with nine peripheral microtubule triplets see structure at bottom center of image . A basal body also called a basal granule or kinetosome is an organelle formed from a centriole , and a short cylindrical array of microtubules . It is found at the base of a eukaryotic undulipodium cilium or flagellum and serves as a nucleation site for the growth of the axoneme microtubules. Centrioles, from which basal bodies are derived, act as anchoring sites for proteins that in turn anchor microtubules within centrosomes , one type of microtubule organizing center MTOC . These microtubules provide structure and facilitate movement of vesicles and organelles within many eukaryotic cells. Basal bodies, however, are specifically the bases for cilia and flagella that extend out of the cell. Basal bodies are derived from centrioles through a largely mysterious process. They are structurally the same, each containing a microtubule triplet 9 3 helocoidal configuration forming a hollow cylinder. Regulation of basal body production and spatial orientation is a function of the nucleotide binding domain of tubulin. ref Y. Shang, C. C. Tsao, and M. A. Gorovsky. 2005. Mutational analyses reveal a novel function of the nucleotide binding domain of gamma tubulin in the regulation of basal body biogenesis. J. Cell Biol. 171 6 1035 44. PMID 16344310 ref Flagella are basically attached to the cell membrane from a basal granule. References reflist External links BUHistology 21804loa Ultrastructure ... more details
Taxobox name Tetrapulmonata image image caption image width 250px status extinct regnum Animal ia phylum Arthropod a classis Arachnid a unranked ordo Tetrapulmonata unranked ordo authority Shultz, 1990 subdivision ranks Orders subdivision Uropygid Thelyphonida Schizomida Amblypygi Spider Araneae Tetrapulmonata is a non ranked supra ordinal group of Arachnida arachnids . It is composed of Uropygid Thelyphonida , Schizomid a, Amblypygid Amblypygi and Spider Araneae . Etymology It receives its name from the presence of paired book lung s occupying the second and third opisthosomal segments, although the posterior pair is absent in Schizomida. Previous synonym s of this lineage are rejected Caulogastra small Pocock, 1983 small refers to pedicel , which is Symplesiomorphy symplesiomorphic for the lineage and Convergent evolution convergent with Solifugae , and Arachnidea small Van der Hammen, 1977 small is easily confused with Arachnid a. Types Other Synapomorphy synapomorphies of Tetrapulmonata include a large postcerebral pharynx reduced in Uropygi , prossomal endosternite with four segmental components, subchelate chelicerae , a complex coxotrochanteral joint in the walking legs, a pretarsal depressor muscle arising in the patella convergent with Dromopoda, lost in Amblypygi , a pedicel formed, in part, by ventral elements of the second opisthomal segment and a spermatozoon axoneme a 9 3 microtubule arrangement. ref cite journal author Jeffrey W. Shultz year 1990 title Evolutionary morphology and phylogeny of Arachnida journal Cladistics journal Cladistics volume 6 issue 1 pages 1 38 doi 10.1111 j.1096 0031.1990.tb00523.x ref References reflist Category Arachnids ca Tetrapulmonat es Tetrapulmonata ... more details
Taxobox domain Eukaryote Eukaryota regnum Chromalveolata superphylum Alveolata phylum Perkinsozoa classis Perkinsea ordo familia Rastromonadida genus Parvilucifera subdivision ranks Species subdivision Parvilucifera infectans br Parvilucifera prorocentri br Parvilucifera sinerae br Parvilucifera is a genus of marine parasitic protozoa that parasitise dinoflagellate s. History The genus was first described by Noren and Moestrup in 1999 and was isolated off the west coast of Sweden . ref name Noren1999 Noren F, Moestrup & Rehnstam Holm A S 1999 Parvilucifera infectans Noren et Moestrup gen et sp nov Perkinsozoa phylum nov a parasitic agellate capable of killing toxic microalgae. Eur J Protistol 35 233 254 ref Taxonomy There are three recognised species in this genus. The type species is Parvilucifera infectans . Description The zoospores are 1.2 1.8 micrometers in diameter and possess two flagella e an anterior transverse one and a shorter posterior one. They also possess alveoli, a refractile body, a mitochondrion with tubular cristae, microneme s, rhoptry rhoptries and a pseudo conoid . They also have a heteromorphic pair of central microtubule s in the anterior axoneme . The micronemes have bulbous posterior ends and are associated with the pseudoconoid. Life cycle Zoospores the infectious stage enter the host cells wherein they develop into round bodies sporangia . The immature sporangia are 5 15 micrometers in diameter and contain spherical bodies and amorphous spaces. The mature sporangia are 20 25 micrometers in diameter when they become enveloped by a wall with a convoluted mid layer. The mature, dark colored sporangia are released from the dead dinoflagellate cells by the break up of the host s theca . The sporangial cytoplasm divides into many minute zoospores which after their release subsequently infect new hosts. The zoospores escape from the cyst through a germ tube 4 5 micrometers in diameter and 10 15 micrometers in length. References reflist Alveol ... more details
PBB geneid 81492 Radial spoke head protein 6 homolog A RSPH6A also known as radial spoke head like protein 1 RSHL1 is a protein that in humans is encoded by the RSPH6A gene . ref name pmid11237735 cite journal author Eriksson M, Ansved T, Anvret M, Carey N title A mammalian radial spokehead like gene, RSHL1, at the myotonic dystrophy 1 locus journal Biochem Biophys Res Commun volume 281 issue 4 pages 835 41 year 2001 month Mar pmid 11237735 pmc doi 10.1006 bbrc.2001.4465 ref ref name entrez Function Radial spoke head protein 6 homolog A is similar to a sea urchin radial spoke head protein. Radial spoke protein complexes form part of the axoneme of eukaryotic flagella and are located between the axoneme s outer ring of doublet microtubule s and central pair of microtubules. In Chlamydomonas , radial spoke proteins are thought to regulate the activity of dynein and the symmetry of flagellar bending patterns. ref name entrez cite web title Entrez Gene RSHL1 radial spokehead like 1 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 81492 accessdate ref Clinical significance The RSPH6A gene maps to a region of chromosome 19 that is linked to primary primary ciliary dyskinesia ciliary dyskinesia 2 CILD2 . ref name entrez References reflist Further reading refbegin 2 cite journal author Maruyama K, Sugano S title Oligo capping a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. journal Gene volume 138 issue 1 2 pages 171 4 year 1994 pmid 8125298 doi 10.1016 0378 1119 94 90802 8 cite journal author Suzuki Y, Yoshitomo Nakagawa K, Maruyama K, et al. title Construction and characterization of a full length enriched and a 5 end enriched cDNA library. journal Gene volume 200 issue 1 2 pages 149 56 year 1997 pmid 9373149 doi 10.1016 S0378 1119 97 00411 3 cite journal author Hartley JL, Temple GF, Brasch MA title DNA cloning using in vitro site specific recombination. journal Genome Res. volume 10 issue 11 pa ... more details
particles along the doublet microtubules of the flagellar axoneme , between the axoneme and the plasma ... particles carry axonemal subunits to the site of assembly at the tip of the axoneme thus, IFT is necessary for axonemal growth. Therefore, since the axoneme needs a continually fresh supply of proteins, an axoneme with defective IFT machinery will slowly shrink in the absence of replacement protein subunits. In healthy flagella, IFT particles reverse direction at the tip of the axoneme, and are thought ... more details
can be divided into two groups cytoplasm ic dyneins and axoneme axonemal dyneins, which are also ... of microtubules in the axoneme s of cilia and flagella and is found only in cells that have those .... Axonemal dynein File Eukaryotic flagellum.svg thumb 200px A cross section of an axoneme, with axonemal ... microtubule of the same axoneme . Each dynein molecule thus forms a cross bridge between two adjacent microtubules of the ciliary axoneme. During the power stroke , which causes movement ... more details
based cytoskeleton called the axoneme . The axoneme of primary cilia typically has a ring of nine outer microtubule triplets called a 9 0 axoneme , and the axoneme of a motile cilium has two central microtubule singlets in addition to the nine outer doublets called a 9 2 axoneme . The axonemal .... A transition zone between the basal body and the axoneme serves as a docking station for intraflagellar ... more details
Image Complete diagram of a human spermatozoa en.svg thumb 300px Complete diagram of a human spermatozoon Spermiogenesis is the final stage of spermatogenesis , which sees the maturation of spermatid s into mature, motile spermatozoon spermatozoa . The spermatid is more or less circular cell containing a nucleus, Golgi apparatus, centriole and mitochondria. All these components take part in forming the spermatozoon. Phases The process of spermiogenesis is traditionally divided into four stages the Golgi phase, the cap phase,formation of tail , and the maturation stage. ref http anatomy.iupui.edu courses histo D502 D502f04 lecture.f04 Malef04 Male 20Reproduction 06.htm ANAT D502 Basic Histology Bot generated title ref Golgi phase The spermatids, which up until now have been mostly Symmetry biology radially symmetrical , begin to develop polarity. The head forms at one end, and the Golgi apparatus creates enzymes that will become the acrosome . At the other end, it develops a thickened mid piece, where the mitochondrium mitochondria gather and the distal centriole begins to form an axoneme . Spermatid DNA also undergoes packaging, becoming highly condensed. The DNA is packaged first, with specific nuclear basic proteins, which are subsequently replaced with protamine s during spermatid elongation. The resultant tightly packed chromatin is transcriptionally inactive. Cap phase The Golgi apparatus surrounds the condensed nucleus, becoming the acrosome acrosomal cap . Image Gray1150.png thumb 300px Note how the tails of the sperm point inward. This orientation occurs during the acrosomal phase. Formation of Tail One of the centriole s of the cell elongates to become the tail of the sperm. A temporary structure called the manchette assists in this elongation. During this phase, the developing spermatozoa orient themselves so that their tails point towards the center of the lumen, away from the epithelium. Maturation phase The excess cytoplasm , known as residual bodies , ... more details
PBB geneid 345895 Radial spoke head protein 4 homolog A , also known as radial spoke head like protein 3 , is a protein that in humans is encoded by the RSPH4A gene . ref name entrez cite web title Entrez Gene radial spoke head 4 homolog A Chlamydomonas url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 345895 accessdate ref ref name pmid19200523 cite journal author Castleman VH, Romio L, Chodhari R, Hirst RA, de Castro SC, Parker KA, Ybot Gonzalez P, Emes RD, Wilson SW, Wallis C, Johnson CA, Herrera RJ, Rutman A, Dixon M, Shoemark A, Bush A, Hogg C, Gardiner RM, Reish O, Greene ND, O Callaghan C, Purton S, Chung EM, Mitchison HM title Mutations in radial spoke head protein genes RSPH9 and RSPH4A cause primary ciliary dyskinesia with central microtubular pair abnormalities journal Am. J. Hum. Genet. volume 84 issue 2 pages 197 209 year 2009 month February pmid 19200523 pmc 2668031 doi 10.1016 j.ajhg.2009.01.011 url issn ref Function TRadial spoke head protein 4 homolog A appears to be a component the radial spoke head, as determined by homology to similar proteins in the biflagellate alga Chlamydomonas reinhardtii and other ciliates. Radial spokes, which are regularly spaced along cilia , sperm, and flagella axoneme s, consist of a thin stalk and a bulbous head that form a signal transduction scaffold between the central pair of microtubule s and dynein . ref name entrez Clinical significance Mutations in the RSPH4A gene are associated with primary ciliary dyskinesia . ref name pmid19200523 References reflist Further reading refbegin 2 cite journal author Bonaldo MF, Lennon G, Soares MB title Normalization and subtraction two approaches to facilitate gene discovery. journal Genome Res. volume 6 issue 9 pages 791 806 year 1996 pmid 8889548 doi 10.1101 gr.6.9.791 cite journal author Strausberg RL, Feingold EA, Grouse LH, et al. title Generation and initial analysis of more than 15,000 full length human and mouse cDNA sequences. journal ... more details
Orphan date February 2009 PBB geneid 140732 Sperm associated antigen 4 like protein is a protein that in humans is encoded by the SPAG4L gene . ref name pmid9691178 cite journal author Tarnasky H, Gill D, Murthy S, Shao X, Demetrick DJ, van der Hoorn FA title A novel testis specific gene, SPAG4, whose product interacts specifically with outer dense fiber protein ODF27, maps to human chromosome 20q11.2 journal Cytogenet Cell Genet volume 81 issue 1 pages 65 7 year 1998 month Oct pmid 9691178 pmc doi 10.1159 000014990 ref ref name pmid10373309 cite journal author Shao X, Tarnasky HA, Lee JP, Oko R, van der Hoorn FA title Spag4, a novel sperm protein, binds outer dense fiber protein Odf1 and localizes to microtubules of manchette and axoneme journal Dev Biol volume 211 issue 1 pages 109 23 year 1999 month Jul pmid 10373309 pmc doi 10.1006 dbio.1999.9297 ref ref name entrez cite web title Entrez Gene SPAG4L sperm associated antigen 4 like url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 140732 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Kierszenbaum AL, Tres LL title Bypassing natural sperm selection during fertilization the azh mutant offspring experience and the alternative of spermiogenesis in vitro. journal Mol. Cell. Endocrinol. volume 187 issue 1 2 pages 133 8 year 2003 pmid 11988320 doi 10.1016 S0303 7207 01 00692 X cite journal author Gerhard DS, Wagner L, Feingold EA, et al. title The status, quality, and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC journal Genome Res. volume 14 issue 10B pages 2121 7 year 2004 pmid 15489334 doi 10.1101 gr.2596504 pmc 528928 cite journal author Ota T, Suzuki Y, Nishikawa T, et al. title Complete sequencing and characterization of 21,243 full ... more details
big Ciliogenesis big is defined as the building of the cell s antenna or cilia . It includes the assembly and disassembly of the cilia during the cell cycle . Cilia are important organelles of cells and are involved in numerous activities such as cell signaling , processing developmental signals, and directing the flow of fluids such as mucus over and around cells. Due to the importance of these cell processes, defects in ciliogenesis can lead to numerous human diseases related to non functioning cilia. ref name nature Ishikawa, H., & Marshall, W. 2011 . Ciliogenesis building the cell s antenna. Molecular Cell Biology, 12, 222 234 . Retrieved from http www.nature.com nrm journal v12 n4 full nrm3085.html ref Mechanisms Ciliogenesis occurs through an ordered set of steps. First, the basal bodies from centrioles must migrate to the surface of the cell and attach to the cortex . Along the way, the basal bodies attach to membrane vesicles and the basal body membrane vesicle complex fuses with the plasma membrane of the cell. Fusion with the plasma membrane is likely what forms the membrane of the cilia. The alignment of the forming cilia is determined by the original positioning and orientation of the basal bodies. Once the alignment is determined, Axoneme axonemal microtubules extend from the basal body and go beneath the developing ciliary membrane, forming the cilia. ref name nature Proteins must be synthesized in the cytoplasm of the cell and cannot be synthesized within cilia. For the cilium to elongate, proteins must be selectively imported from the cytoplasm into the cilium and transported to the tip of the cilium by intraflagellar transport ITF . Once the cilium is completely formed, it continues to incorporate new tubulin at the tip of the cilia. However, the cilium does not elongate further, because older tubulin is simultaneously degraded. This requires an active mechanism that maintains ciliary length. Impairments in these mechanisms can affect the motility o ... more details
assembly and maintenance.2C and function structurally different 9 0 axoneme rather than the 9 2 axoneme found in both flagella and motile cilia undulopodia. Bacterial Image Flagellum base diagram ... Eukarya Flagella.svg thumb left Eukaryotic flagella. 1 axoneme, 2 cell membrane, 3 IFT IntraFlagellar ... Eukaryotic flagellum.svg thumb 200px Cross section of an axoneme Image Chlamydomonas TEM 09.jpg ... in this cross section micrograph of axoneme Along with cilia , flagella make up a group of organelles ... of the core of the eukaryotic flagellum called an axoneme . At the base of a eukaryotic flagellum ... produce force through ATP hydrolysis . The flagellar axoneme also contains radial spoke s, polypeptide ... more details
For the Canadian politician Keith Porter politician as Keith Porter redirects here Keith Roberts Porter 1912 1997 was a Canada Canadian Cell biology cell biologist . He did pioneering biology research using electron microscope electron microscopy of Cell biology cells ref name Cooper2000 cite book chapter Ch. 1 Section Electron Microscopy chapterurl http www.ncbi.nlm.nih.gov books NBK9941 A139 author Cooper, Geoffrey M. title The Cell A Molecular Approach publisher Sinauer Associates location Sunderland MA year 2000 isbn 0 87893 106 6 edition 2nd url http www.ncbi.nlm.nih.gov books NBK9839 ref , such as work on the 9 2 microtubule structure in the axoneme of cilia . Porter also contributed to the development of other experimental methods for cell culture and Somatic cell nuclear transfer nuclear transplantation . He also was responsible for naming the endoplasmic reticulum ref name jexpmed porter cite journal author Porter KR, Claude A, Fullam EF title A Study of Tissue Culture Cells by Electron Microscopy journal J Exp Med. year 1945 pages 233 246 volume 81 issue 3 url http www.jem.org cgi content abstract 81 3 233 doi 10.1084 jem.81.3.233 pmid 19871454 pmc 2135493 ref . Keith Porter was born in Yarmouth, Nova Scotia Yarmouth , Nova Scotia on June 11, 1912, and became a citizen of the United States in 1947. He was an undergraduate at Acadia University and a graduate student at Harvard University . Starting in the late 1930s he did research at The Rockefeller University The Rockefeller Institute for Medical Research . Porter helped found the American Society for Cell Biology and the Journal of Cell Biology. The Keith R. Porter Endowment for Cell Biology, founded in 1981, supports an annual Keith R. Porter Lecture at the conference of American Society for Cell Biology . ref http porterendowment.org Keith R. Porter Endowment for Cell Biology ref Porter moved to Harvard University in 1961 and to the University of Colorado at Boulder University of Colorado at Boulder, C ... more details
PBB geneid 4957 Outer dense fiber protein 2 , also known as cenexin , is a protein that in humans is encoded by the ODF2 gene . ref name pmid9045620 cite journal author Shao X, Tarnasky HA, Schalles U, Oko R, van der Hoorn FA title Interactional cloning of the 84 kDa major outer dense fiber protein Odf84. Leucine zippers mediate associations of Odf84 and Odf27 journal J Biol Chem volume 272 issue 10 pages 6105 13 year 1997 month Apr pmid 9045620 pmc doi 10.1074 jbc.272.10.6105 ref ref name pmid10072582 cite journal author Shao X, Murthy S, Demetrick DJ, van der Hoorn FA title Human outer dense fiber gene, ODF2, localizes to chromosome 9q34 journal Cytogenet Cell Genet volume 83 issue 3 4 pages 221 3 year 1999 month Mar pmid 10072582 pmc doi 10.1159 000015183 ref ref name entrez cite web title Entrez Gene ODF2 outer dense fiber of sperm tails 2 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 4957 accessdate ref The PBB Summary template is automatically maintained by Protein Box Bot. See Template PBB Controls to Stop updates. PBB Summary section title summary text The outer dense fibers are cytoskeletal structures that surround the axoneme in the middle piece and principal piece of the sperm tail. The fibers function in maintaining the elastic structure and recoil of the sperm tail as well as in protecting the tail from shear forces during epididymal transport and ejaculation. Defects in the outer dense fibers lead to abnormal sperm morphology and infertility. This gene encodes one of the major outer dense fiber proteins. Multiple protein isoforms are encoded by transcript variants of this gene however, not all isoforms and variants have been fully described. ref name entrez References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Kierszenbaum AL title Keratins unraveling the coordinated construction of scaffolds in spermatogenic cells journal Mol. Reprod. Dev. volume 61 issue 1 pages 1 2 year 2 ... more details
PBB geneid 8701 Dynein heavy chain 11, axonemal is a protein that in humans is encoded by the DNAH11 gene . ref name pmid9256245 cite journal author Chapelin C, Duriez B, Magnino F, Goossens M, Escudier E, Amselem S title Isolation of several human axonemal dynein heavy chain genes genomic structure of the catalytic site, phylogenetic analysis and chromosomal assignment journal FEBS Lett volume 412 issue 2 pages 325 30 year 1997 month Sep pmid 9256245 pmc doi 10.1016 S0014 5793 97 00800 4 ref ref name entrez cite web title Entrez Gene DNAH11 dynein, axonemal, heavy chain 11 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 8701 accessdate ref Function This gene encodes a member of the dynein heavy chain family. It is a microtubule dependent motor ATPase and has been reported to be involved in the movement of respiratory cilia. Mutations in this gene have been implicated in causing primary ciliary dyskinesia PCD, formerly called immotile cilia syndrome and Kartagener syndrome PCD with situs inversus totalis . Males with PCD are not sterile, but are infertile due to lack of sperm motility. ref name entrez cite web title Entrez Gene DNAH11 dynein, axonemal, heavy chain 11 url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 8701 accessdate ref . There are reports of subfertility and increased risk of ectopic pregnancy in women with PCD. ref cite journal author Blyth M, Wellesley D title Ectopic pregnancy in primary ciliary dyskinesia journal J Obstet Gynaecol volume 28 issue 3 pages 358 year 2008 month April pmid 18569496 doi 10.1080 01443610802058742 url ref References reflist Further reading refbegin 2 PBB Further reading citations cite journal author Schwabe GC, Hoffmann K, Loges NT, et al. title Primary ciliary dyskinesia associated with normal axoneme ultrastructure is caused by DNAH11 mutations. journal Hum. Mutat. volume 29 issue 2 pages 289 98 year 2008 pmid 18022865 doi 10.1002 humu.20656 cite jour ... more details
PBB geneid 11127 Kinesin like protein KIF3A is a protein that in humans is encoded by the KIF3A gene . ref name pmid10548469 cite journal author Whitehead JL, Wang SY, Bost Usinger L, Hoang E, Frazer KA, Burnside B title Photoreceptor localization of the KIF3A and KIF3B subunits of the heterotrimeric microtubule motor kinesin II in vertebrate retina journal Exp. Eye Res. volume 69 issue 5 pages 491 503 year 1999 month November pmid 10548469 doi 10.1006 exer.1999.0724 ref ref name entrez cite web title Entrez Gene KIF3A kinesin family member 3A url http www.ncbi.nlm.nih.gov sites entrez?Db gene&Cmd ShowDetailView&TermToSearch 11127 accessdate ref Function KIF3A is one subunit of the protein trimer heterotrimeric motor protein, kinesin 2, that was initially isolated from sea urchin egg embryo cytosol using microtubule affinity purification. ref name pmid8232586 cite journal author Cole DG, Chinn SW, Wedaman KP, Hall K, Vuong T, Scholey JM title Novel heterotrimeric kinesin related protein purified from sea urchin eggs journal Nature volume 366 issue 6452 pages 268 70 year 1993 month November pmid 8232586 doi 10.1038 366268a0 ref This motor consists of two kinesin related subunits called KIF3A and KIF3B or 3C in vertebrates and an associated protein KIFAP3 KAP3 , and it transports protein complexes, nucleic acids and organelles towards the plus ends of microtubule tracks within cells. Work done in a broad range of eukaryotic cells has revealed that heterotrimeric kinesin 2 is the primary motor protein driving the intra flagellum flagellar transport of tubulin s and other axoneme axonemal building blocks from the base of the ciliary flagellar axoneme to their site of assembly at the distal tips. ref name pmid12415299 cite journal author Rosenbaum JL, Witman GB title Intraflagellar transport journal Nat. Rev. Mol. Cell Biol. volume 3 issue 11 pages 813 25 year 2002 month November pmid 12415299 doi 10.1038 nrm952 ref This process is required for cilium assembly maintenanc ... more details
Taxobox name Alveolata image Ceratium furca.jpg image caption Ceratium furca fossil range Ediacaran ref cite journal first C. W. last Li coauthors et al. title Ciliated protozoans from the Precambrian Doushantuo Formation, Wengan, South China journal Geological Society, London, Special Publications year 2007 volume 286 pages 151 156 doi 10.1144 SP286.11 ref Recent domain Eukarya regnum Chromalveolata superphylum Alveolata subdivision ranks Phyla subdivision Apicomplexa br Chromerida br Ciliophora br Dinoflagellate Dinoflagellata br The alveolates with cavities ref cite web url http www.memidex.com alveolate title alveolate work Memidex WordNet Dictionary Thesaurus accessdate 2011 01 26 ref are a major line of protist s. Phyla There are four phylum phyla , which are very divergent in form, but are now known to be close relatives based on various ultrastructural and genetic similarities Apicomplexa parasitic protozoa that lack Axoneme axonemal locomotive structures except in gamete s Chromerida a marine phylum of photosynthetic protozoa Ciliate s very common protozoa with many short cilium cilia arranged in rows Dinoflagellate s mostly marine flagellate s many of which have chloroplast s The genus Perkinsus may belong to another clade Perkinsozoa based on a number of molecular biological findings. ref name Zhang2011 Zhang H, Campbell DA, Sturm NR, Dungan CF, Lin S 2011 Spliced leader RNAs, mitochondrial gene frameshifts and multi protein phylogeny expand support for the genus Perkinsus as a unique group of Alveolates. PLoS One. 2011 6 5 e19933 ref Characteristics The most notable shared characteristic is the presence of cortical alveoli, flattened vesicle biology vesicle s packed into a continuous layer supporting the cell membrane membrane , typically forming a flexible pellicle. In dinoflagellates they often form armor plates. Alveolates have mitochondrion mitochondria with tubular cristae and their flagella or cilia have a distinct structure. The ancestors of this ... more details
Encyclopedia
top
