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2n12

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Revision as of 17:13, 15 August 2018

Solution structure of human Myosin VI isoform3 (1050-1131)

Structural highlights

2n12 is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2n0z, 2n10, 2n11, 2n13
Gene:	MYO6, KIAA0389 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Publication Abstract from PubMed

Myosin VI functions in endocytosis and cell motility. Alternative splicing of myosin VI mRNA generates two distinct isoform types, myosin VIshort and myosin VIlong, which differ in the C-terminal region. Their physiological and pathological roles remain unknown. Here we identified an isoform-specific regulatory helix, named the alpha2-linker, that defines specific conformations and hence determines the target selectivity of human myosin VI. The presence of the alpha2-linker structurally defines a new clathrin-binding domain that is unique to myosin VIlong and masks the known RRL interaction motif. This finding is relevant to ovarian cancer, in which alternative myosin VI splicing is aberrantly regulated, and exon skipping dictates cell addiction to myosin VIshort in tumor-cell migration. The RRL interactor optineurin contributes to this process by selectively binding myosin VIshort. Thus, the alpha2-linker acts like a molecular switch that assigns myosin VI to distinct endocytic (myosin VIlong) or migratory (myosin VIshort) functional roles.

Diverse functions of myosin VI elucidated by an isoform-specific alpha-helix domain.,Wollscheid HP, Biancospino M, He F, Magistrati E, Molteni E, Lupia M, Soffientini P, Rottner K, Cavallaro U, Pozzoli U, Mapelli M, Walters KJ, Polo S Nat Struct Mol Biol. 2016 Apr;23(4):300-8. doi: 10.1038/nsmb.3187. Epub 2016 Mar , 7. PMID:26950368^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ Wollscheid HP, Biancospino M, He F, Magistrati E, Molteni E, Lupia M, Soffientini P, Rottner K, Cavallaro U, Pozzoli U, Mapelli M, Walters KJ, Polo S. Diverse functions of myosin VI elucidated by an isoform-specific alpha-helix domain. Nat Struct Mol Biol. 2016 Apr;23(4):300-8. doi: 10.1038/nsmb.3187. Epub 2016 Mar , 7. PMID:26950368 doi:http://dx.doi.org/10.1038/nsmb.3187

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2n12"

Categories: Human | He, F | Walters, K | Motor protein | Protein transport

@@ Line 3: / Line 3: @@
 <StructureSection load='2n12' size='340' side='right' caption='[[2n12]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2n12]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N12 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2n12]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N12 FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2n0z|2n0z]], [[2n10|2n10]], [[2n11|2n11]], [[2n13|2n13]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n12 OCA], [http://pdbe.org/2n12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n12 RCSB], [http://www.ebi.ac.uk/pdbsum/2n12 PDBsum]</span></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO6, KIAA0389 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n12 OCA], [http://pdbe.org/2n12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n12 RCSB], [http://www.ebi.ac.uk/pdbsum/2n12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n12 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 24: / Line 25: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: He, F]]
 [[Category: Walters, K]]
 [[Category: Motor protein]]
 [[Category: Protein transport]]

2n12

From Proteopedia

Revision as of 17:13, 15 August 2018

Solution structure of human Myosin VI isoform3 (1050-1131)

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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