MYO6

Last updated
MYO6
Protein MYO6 PDB 2bkh.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases MYO6 , DFNA22, DFNB37, myosin VI, Myo6-008, Myo6-007
External IDs OMIM: 600970 MGI: 104785 HomoloGene: 56417 GeneCards: MYO6
Gene location (Human)
Ideogram human chromosome 6.svg
Chr. Chromosome 6 (human) [1]
Human chromosome 6 ideogram.svg
HSR 1996 II 3.5e.svg
Red rectangle 2x18.png
Band 6q14.1Start75,749,192 bp [1]
End75,919,537 bp [1]
RNA expression pattern
PBB GE MYO6 210480 s at fs.png

PBB GE MYO6 203216 s at fs.png

PBB GE MYO6 203215 s at fs.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001039546
NM_008662

RefSeq (protein)

n/a

Location (UCSC) Chr 6: 75.75 – 75.92 Mb Chr 9: 80.17 – 80.31 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Myosin VI, also known as MYO6, is a protein. It has been found in humans, mice, fruit flies ( Drosophila melanogaster ), and nematodes ( Caenorhabditis elegans ).

Function

Myosin VI is a molecular motor involved in intracellular vesicle and organelle transport. It is one of the so-called unconventional myosins.[supplied by OMIM] [5]

Interactions

MYO6 has been shown to interact with GIPC1, [6] [7] DAB2., [8] [9] ubiquitin, [10] and clathrin [11]

Related Research Articles

Endocytosis Cellular process

Endocytosis is a cellular process in which substances are brought into the cell. The material to be internalized is surrounded by an area of cell membrane, which then buds off inside the cell to form a vesicle containing the ingested material. Endocytosis includes pinocytosis and phagocytosis. It is a form of active transport.

Myosin

Myosins are a superfamily of motor proteins best known for their roles in muscle contraction and in a wide range of other motility processes in eukaryotes. They are ATP-dependent and responsible for actin-based motility. The term was originally used to describe a group of similar ATPases found in the cells of both striated muscle tissue and smooth muscle tissue. Following the discovery by Pollard and Korn (1973) of enzymes with myosin-like function in Acanthamoeba castellanii, a global range of divergent myosin genes have been discovered throughout the realm of eukaryotes.

Clathrin Protein playing a major role in the formation of coated vesicles

Clathrin is a protein that plays a major role in the formation of coated vesicles. Clathrin was first isolated and named by Barbara Pearse in 1976. It forms a triskelion shape composed of three clathrin heavy chains and three light chains. When the triskelia interact they form a polyhedral lattice that surrounds the vesicle, hence the protein's name, which is derived from the Latin clathrum meaning lattice. Coat-proteins, like clathrin, are used to build small vesicles in order to transport molecules within cells. The endocytosis and exocytosis of vesicles allows cells to communicate, to transfer nutrients, to import signaling receptors, to mediate an immune response after sampling the extracellular world, and to clean up the cell debris left by tissue inflammation. The endocytic pathway can be hijacked by viruses and other pathogens in order to gain entry to the cell during infection.

MYO7A

Myosin VIIA is protein that in humans is encoded by the MYO7A gene. Myosin VIIA is a member of the unconventional myosin superfamily of proteins. Myosins are actin binding molecular motors that use the enzymatic conversion of ATP - ADP + inorganic phosphate (Pi) to provide the energy for movement.

MYO5A

Myosin-Va (MYO5A) is a motor protein in charge of the intracellular transport of vesicles, organelles and protein complexes along the actin filaments. MYO5A gene encodes for the unconventional Myosin motor Va.

DAB2

Disabled homolog 2 is a protein that in humans is encoded by the DAB2 gene.

AP1M1

AP-1 complex subunit mu-1 is a protein that in humans is encoded by the AP1M1 gene.

DNM1

Dynamin-1 is a protein that in humans is encoded by the DNM1 gene.

WIPF1

WAS/WASL-interacting protein family member 1 (WIP) is a protein that in humans is encoded by the WIPF1 gene.

MYO9B

MYO9B is a gene that encodes the Myosin-IXb protein.

MYO1C

Myosin-Ic is a protein that in humans is encoded by the MYO1C gene.

MYO10

Myosin X, also known as MYO10, is a protein that in humans is encoded by the MYO10 gene.

MYO1A

Myosin-Ia is a protein that in humans is encoded by the MYO1A gene.

MYO18A

Myosin-XVIIIa is a protein that in humans is encoded by the MYO18A gene.

MYO5B

Myosin-Vb, a myosin V type protein, is encoded by the MYO5B gene in humans.

MYO3A

Myosin IIIA is a protein that in humans is encoded by the MYO3A gene.

MYO1B

Myosin-Ib is a protein that in humans is encoded by the MYO1B gene.

MYO1F

Myosin-If is a protein that in humans is encoded by the MYO1F gene.

MYO18B

Myosin-XVIIIb is a protein that in humans is encoded by the MYO18B gene.

MYO1E

Myosin-Ie (Myo1e) is a protein that in humans is encoded by the MYO1E gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000196586 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033577 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: MYO6 myosin VI".
  6. Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.
  7. Sennacherib L, Lee T, Hasson T (Jul 2003). "Myo6 facilitates the translocation of endocytic vesicles from cell peripheries". Molecular Biology of the Cell. 14 (7): 2728–43. doi:10.1091/mbc.E02-11-0767. PMC   165672 . PMID   12857860.
  8. Morris SM, Arden SD, Roberts RC, Kendrick-Jones J, Cooper JA, Luzio JP, Buss F (May 2002). "Myosin VI binds to and localises with Dab2, potentially linking receptor-mediated endocytosis and the actin cytoskeleton". Traffic. 3 (5): 331–41. doi:10.1034/j.1600-0854.2002.30503.x. PMID   11967127. S2CID   25079713.
  9. Inoue A, Sato O, Homma K, Ikebe M (Mar 2002). "DOC-2/DAB2 is the binding partner of myosin VI". Biochemical and Biophysical Research Communications. 292 (2): 300–7. doi:10.1006/bbrc.2002.6636. PMID   11906161.
  10. He F, Wollscheid HP, Nowicka U, Biancospino M, Valentini E, Ehlinger A, Acconcia F, Magistrati E, Polo S, Walters KJ (2016). "Myosin VI Contains a Compact Structural Motif that Binds to Ubiquitin Chains". Cell Reports. 14 (11): 2683–94. doi:10.1016/j.celrep.2016.01.079. PMC   4805485 . PMID   26971995.
  11. Biancospino M, Buel GR, Niño CA, Maspero E, di Perrotolo RS, Raimondi A, Redlingshöfer L, Weber J, Brodsky FM, Walters KJ, Polo S (2019). "Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension". Nature Communications. 10 (1): 4974. Bibcode:2019NatCo..10.4974B. doi:10.1038/s41467-019-12855-6. PMC   6823378 . PMID   31672988.

Further reading