Vinculin
From Proteopedia
Jump to navigationJump to search
| ||||||||||||
- Created with the participation of Susan Craig.
ContentsFunctionVinculins (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 highlightsVinculin Autoinhibition 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 VinculinReferences
| ||||||||||||
This page was last modified 08:07, 19 March 2024.