Vinculin: Difference between revisions
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*Metavinculin; Domains - head 1-256; tail 959-1134 | *Metavinculin; Domains - head 1-256; tail 959-1134 | ||
**[[6fuy]] - | **[[6fuy]] - hVCL <br /> | ||
**[[3rf3]] - | **[[3rf3]] - hVCL head domain + invasin IPAA<br /> | ||
**[[3s90]] - | **[[3s90]] - hVCL head domain + mTalin-1 peptide<br /> | ||
**[[4dj9]] - | **[[4dj9]] - hVCL head domain + hTalin-1 peptide <br /> | ||
**[[6fq4]] - | **[[6fq4]] - hVCL head domain + TARP peptide <br /> | ||
**[[3tj5]] - | **[[3tj5]] - hVCL head domain + Sca-family protein peptide<br /> | ||
**[[3tj6]] - | **[[3tj6]] - hVCL head domain + protein Ps 120 peptide<br /> | ||
**[[4ehp]], [[5y04]] - | **[[4ehp]], [[5y04]] - hVCL head domain + catenin α-1 residues 277-382<br /> | ||
**[[3myi]] – | **[[3myi]] – hVCL tail domain <br /> | ||
**[[5l0f]], [[5l0i]], [[5l0j]] - | **[[5l0f]], [[5l0i]], [[5l0j]] - hVCL tail domain (mutant)<br /> | ||
**[[5l0c]], [[5l0d]] - | **[[5l0c]], [[5l0d]] - hVCL tail domain + lipid<br /> | ||
**[[5l0g]], [[5l0h]] - | **[[5l0g]], [[5l0h]] - hVCL tail domain (mutant) + lipid<br /> | ||
**[[3jbk]] – | **[[3jbk]] – hVCL tail domain + actin – Cryo-EM<br /> | ||
**[[3vf0]] – | **[[6upw]] - mVCL head domain + catenin α-1<br /> | ||
**[[1st6]] – | **[[3vf0]] – hVCL tail domain + ribonucleoprotein PTB-binding<br /> | ||
**[[2gdc]] – | **[[1st6]] – cVCL<br /> | ||
**[[1xwj]] - | **[[2gdc]] – cVCL head domain +SfInvasin C-terminal <br /> | ||
**[[1zvz]], [[1zw2]], [[1zw3]], [[1u6h]] - | **[[1xwj]] - cVCL head domain +cTalin VBS3<br /> | ||
**[[6fq4]] – | **[[1zvz]], [[1zw2]], [[1zw3]], [[1u6h]] - cVCL head domain +cTalin rod<br /> | ||
**[[4e17]], [[4e18]] - | **[[6fq4]] – cVCL head domain + TARP-VBS1<br /> | ||
**[[4e17]], [[4e18]] - cVCL head domain + catenin α-1 VCL-binding domain | |||
}} | }} | ||
==References== | ==References== | ||
Revision as of 12:06, 11 January 2021
FunctionVinculins (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. RelevanceLoss of VCL could be used as a prognostic factor for colorectal cancer se it promotes metastasis[2]. DiseaseMutation in m-VCL can yield cardiomyopathic phenotype[3]. Structural highlightsis achieved through a high affinity intramolecular interaction between tail (orange) and head (aqua) domains (1st6). Energetically, I997 is key to maintaining this autoinhibition. |
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3D Structures of Vinculin3D Structures of Vinculin
Updated on 11-January-2021
ReferencesReferences
- ↑ 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
- ↑ 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
- ↑ 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.