6e5n

Structural highlights

Disease

[MYO6_HUMAN] Autosomal dominant non-syndromic sensorineural deafness type DFNA;Autosomal recessive non-syndromic sensorineural deafness type DFNB;Progressive sensorineural hearing loss - hypertrophic cardiomyopathy. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.

Function

[MYO6_HUMAN] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Myosin 6 is a reverse-direction motor protein that moves towards the minus-end of actin filaments. Has slow rate of actin-activated ADP release due to weak ATP binding. Functions in a variety of intracellular processes such as vesicular membrane trafficking and cell migration. Required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. May act as a regulator of F-actin dynamics. May play a role in transporting DAB2 from the plasma membrane to specific cellular targets. Required for structural integrity of inner ear hair cells (By similarity).^{[1] [2] [3] [4]} [CLCA_HUMAN] Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (PubMed:15858577, PubMed:21297582).^{[5] [6]}

References

1. ↑ Wells AL, Lin AW, Chen LQ, Safer D, Cain SM, Hasson T, Carragher BO, Milligan RA, Sweeney HL. Myosin VI is an actin-based motor that moves backwards. Nature. 1999 Sep 30;401(6752):505-8. PMID:10519557 doi:http://dx.doi.org/10.1038/46835
2. ↑ Buss F, Arden SD, Lindsay M, Luzio JP, Kendrick-Jones J. Myosin VI isoform localized to clathrin-coated vesicles with a role in clathrin-mediated endocytosis. EMBO J. 2001 Jul 16;20(14):3676-84. PMID:11447109 doi:http://dx.doi.org/10.1093/emboj/20.14.3676
3. ↑ Jung EJ, Liu G, Zhou W, Chen X. Myosin VI is a mediator of the p53-dependent cell survival pathway. Mol Cell Biol. 2006 Mar;26(6):2175-86. PMID:16507995 doi:http://dx.doi.org/10.1128/MCB.26.6.2175-2186.2006
4. ↑ Vreugde S, Ferrai C, Miluzio A, Hauben E, Marchisio PC, Crippa MP, Bussi M, Biffo S. Nuclear myosin VI enhances RNA polymerase II-dependent transcription. Mol Cell. 2006 Sep 1;23(5):749-55. PMID:16949370 doi:http://dx.doi.org/10.1016/j.molcel.2006.07.005
5. ↑ Royle SJ, Bright NA, Lagnado L. Clathrin is required for the function of the mitotic spindle. Nature. 2005 Apr 28;434(7037):1152-7. doi: 10.1038/nature03502. PMID:15858577 doi:http://dx.doi.org/10.1038/nature03502
6. ↑ Booth DG, Hood FE, Prior IA, Royle SJ. A TACC3/ch-TOG/clathrin complex stabilises kinetochore fibres by inter-microtubule bridging. EMBO J. 2011 Mar 2;30(5):906-19. doi: 10.1038/emboj.2011.15. Epub 2011 Feb 4. PMID:21297582 doi:http://dx.doi.org/10.1038/emboj.2011.15
7. ↑ Biancospino M, Buel GR, Nino CA, Maspero E, Scotto di Perrotolo R, Raimondi A, Redlingshofer L, Weber J, Brodsky FM, Walters KJ, Polo S. Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension. Nat Commun. 2019 Oct 31;10(1):4974. doi: 10.1038/s41467-019-12855-6. PMID:31672988 doi:http://dx.doi.org/10.1038/s41467-019-12855-6