Vinculin

From Proteopedia

Revision as of 21:36, 5 October 2018

spinqualitylabelsall models Chicken full-length metavinculin, 1st6 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Disease 4 Structural highlights Function Vinculins (VCLs) are involved in adhesion by linking integrin molecules to the actin cytoskeleton. Its head domain (Vd1) can bind to talin or to alpha-actinin at their respective VCL Binding Sites (VBS)[1]. The protein raver1 RNA Recognition Motif (RRM) forms a complex with VCL or m-VCL. Metavinculin (m-VCL) is a splice version of VCL containing an extra ca. 70 amino acids in the C-terminal domain. Relevance Loss of VCL could be used as a prognostic factor for colorectal cancer se it promotes metastasis[2]. Disease Mutation in m-VCL can yield cardiomyopathic phenotype[3]. Structural highlights is achieved through a high affinity intramolecular interaction between tail (orange) and head (aqua) domains (1st6). Energetically, I997 is key to maintaining this autoinhibition.

3D Structures of Vinculin

Updated on 05-October-2018

References

1. ↑ Palovuori R, Eskelinen S. Role of vinculin in the maintenance of cell-cell contacts in kidney epithelial MDBK cells. Eur J Cell Biol. 2000 Dec;79(12):961-74. PMID:11152287 doi:http://dx.doi.org/10.1078/0171-9335-00120
2. ↑ Li T, Guo H, Song Y, Zhao X, Shi Y, Lu Y, Hu S, Nie Y, Fan D, Wu K. Loss of vinculin and membrane-bound beta-catenin promotes metastasis and predicts poor prognosis in colorectal cancer. Mol Cancer. 2014 Dec 11;13:263. doi: 10.1186/1476-4598-13-263. PMID:25496021 doi:http://dx.doi.org/10.1186/1476-4598-13-263
3. ↑ Vasile VC, Will ML, Ommen SR, Edwards WD, Olson TM, Ackerman MJ. Identification of a metavinculin missense mutation, R975W, associated with both hypertrophic and dilated cardiomyopathy. Mol Genet Metab. 2006 Feb;87(2):169-74. Epub 2005 Oct 19. PMID:16236538 doi:S1096-7192(05)00258-1

• Created with the participation of Susan Craig.