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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TBB4B_BOVIN TBB4B_BOVIN] Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (PubMed: | [https://www.uniprot.org/uniprot/TBB4B_BOVIN TBB4B_BOVIN] Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (PubMed:2207090, PubMed:6504138, PubMed:7704569). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:2207090, PubMed:6504138, PubMed:7704569).<ref>PMID:2207090</ref> <ref>PMID:6504138</ref> <ref>PMID:7704569</ref> | ||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | |||
*[[Tubulin 3D Structures|Tubulin 3D Structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 17:46, 6 November 2024
bovine sperm endpiece singlet microtubules (one tubulin dimer and associated microtubule inner proteins)bovine sperm endpiece singlet microtubules (one tubulin dimer and associated microtubule inner proteins)
Structural highlights
FunctionTBB4B_BOVIN Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (PubMed:2207090, PubMed:6504138, PubMed:7704569). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:2207090, PubMed:6504138, PubMed:7704569).[1] [2] [3] Publication Abstract from PubMedSperm motility is crucial to reproductive success in sexually reproducing organisms. Impaired sperm movement causes male infertility, which is increasing globally. Sperm are powered by a microtubule-based molecular machine-the axoneme-but it is unclear how axonemal microtubules are ornamented to support motility in diverse fertilization environments. Here, we present high-resolution structures of native axonemal doublet microtubules (DMTs) from sea urchin and bovine sperm, representing external and internal fertilizers. We identify >60 proteins decorating sperm DMTs; at least 15 are sperm associated and 16 are linked to infertility. By comparing DMTs across species and cell types, we define core microtubule inner proteins (MIPs) and analyze evolution of the tektin bundle. We identify conserved axonemal microtubule-associated proteins (MAPs) with unique tubulin-binding modes. Additionally, we identify a testis-specific serine/threonine kinase that links DMTs to outer dense fibers in mammalian sperm. Our study provides structural foundations for understanding sperm evolution, motility, and dysfunction at a molecular level. Structural specializations of the sperm tail.,Leung MR, Zeng J, Wang X, Roelofs MC, Huang W, Zenezini Chiozzi R, Hevler JF, Heck AJR, Dutcher SK, Brown A, Zhang R, Zeev-Ben-Mordehai T Cell. 2023 Jun 22;186(13):2880-2896.e17. doi: 10.1016/j.cell.2023.05.026. Epub , 2023 Jun 15. PMID:37327785[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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