Vinculin: Difference between revisions
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**[[3myi]] – m-VCL tail domain <br /> | **[[3myi]] – m-VCL tail domain <br /> | ||
**[[5l0f]], [[5l0i]], [[ | **[[5l0f]], [[5l0i]], [[5l0j]] - hm-VCL tail domain (mutant)<br /> | ||
**[[5l0c]], [[5l0d]] - hm-VCL tail domain + lipid<br /> | **[[5l0c]], [[5l0d]] - hm-VCL tail domain + lipid<br /> | ||
**[[5l0g]], [[5l0h]] - hm-VCL tail domain (mutant) + lipid<br /> | **[[5l0g]], [[5l0h]] - hm-VCL tail domain (mutant) + lipid<br /> |
Revision as of 12:49, 13 December 2016
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]. 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 13-December-2016
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
- Created with the participation of Susan Craig.