MYO5A

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Myosin VA (heavy chain 12, myoxin)
Protein MYO5A PDB 1oe9.png
PDB rendering based on 1oe9.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols MYO5A ; GS1; MYH12; MYO5; MYR12
External IDs OMIM160777 MGI105976 HomoloGene20100 GeneCards: MYO5A Gene
RNA expression pattern
PBB GE MYO5A 204527 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 4644 17918
Ensembl ENSG00000197535 ENSMUSG00000034593
UniProt Q9Y4I1 Q99104
RefSeq (mRNA) NM_000259 NM_010864
RefSeq (protein) NP_000250 NP_034994
Location (UCSC) Chr 15:
52.6 – 52.82 Mb
Chr 9:
75.07 – 75.22 Mb
PubMed search [1] [2]

Myosin-Va is a protein that in humans is encoded by the MYO5A gene.[1][2][3]


Model organisms[edit]

Model organisms have been used in the study of MYO5A function. A conditional knockout mouse line, called Myo5atm1e(KOMP)Wtsi[9][10] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[11][12][13]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[7][14] Twenty five tests were carried out on mutant mice and three significant abnormalities were observed.[7] Male homozygous mutants had abnormal hair cycles, coat colouration and an increased susceptibility to bacterial infection.[7]

Interactions[edit]

MYO5A has been shown to interact with DYNLL1,[15] RAB27A[16][17] and DYNLL2.[15][18]

Clinical significance[edit]

Defects are associated with Griscelli syndrome type 1, also known as Elejalde syndrome.

See also[edit]

References[edit]

  1. ^ Engle LJ, Kennett RH (June 1994). "Cloning, analysis, and chromosomal localization of myoxin (MYH12), the human homologue to the mouse dilute gene". Genomics 19 (3): 407–16. doi:10.1006/geno.1994.1088. PMID 8188282. 
  2. ^ Bement WM, Hasson T, Wirth JA, Cheney RE, Mooseker MS (August 1994). "Identification and overlapping expression of multiple unconventional myosin genes in vertebrate cell types". Proc Natl Acad Sci U S A 91 (14): 6549–53. doi:10.1073/pnas.91.14.6549. PMC 44240. PMID 8022818. 
  3. ^ "Entrez Gene: MYO5A myosin VA (heavy chain 12, myoxin)". 
  4. ^ "Dysmorphology data for Myo5a". Wellcome Trust Sanger Institute. 
  5. ^ "Salmonella infection data for Myo5a". Wellcome Trust Sanger Institute. 
  6. ^ "Citrobacter infection data for Myo5a". Wellcome Trust Sanger Institute. 
  7. ^ a b c d Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x. 
  8. ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  9. ^ "International Knockout Mouse Consortium". 
  10. ^ "Mouse Genome Informatics". 
  11. ^ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.  edit
  12. ^ Dolgin E (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718. 
  13. ^ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247. 
  14. ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353. 
  15. ^ a b Naisbitt, S; Valtschanoff J; Allison D W; Sala C; Kim E; Craig A M; Weinberg R J; Sheng M (June 2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein". J. Neurosci. (UNITED STATES) 20 (12): 4524–34. ISSN 0270-6474. PMID 10844022. 
  16. ^ Wu, Xufeng; Wang Fei; Rao Kang; Sellers James R; Hammer John A (May 2002). "Rab27a is an essential component of melanosome receptor for myosin Va". Mol. Biol. Cell (United States) 13 (5): 1735–49. doi:10.1091/mbc.01-12-0595. ISSN 1059-1524. PMC 111140. PMID 12006666. 
  17. ^ Nagashima, Kazuaki; Torii Seiji; Yi Zhaohong; Igarashi Michihiro; Okamoto Koichi; Takeuchi Toshiyuki; Izumi Tetsuro (April 2002). "Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions". FEBS Lett. (Netherlands) 517 (1–3): 233–8. doi:10.1016/S0014-5793(02)02634-0. ISSN 0014-5793. PMID 12062444. 
  18. ^ Puthalakath, H; Villunger A; O'Reilly L A; Beaumont J G; Coultas L; Cheney R E; Huang D C; Strasser A (September 2001). "Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis". Science (United States) 293 (5536): 1829–32. doi:10.1126/science.1062257. ISSN 0036-8075. PMID 11546872. 

Further reading[edit]