Vinculin: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
Line 17: Line 17:


**[[1tr2]] – hVCL - human<br />
**[[1tr2]] – hVCL - human<br />
**[[1qkr]] – hVCL C-terminal<br />
**[[1qkr]] – hVCL tail domain<br />
**[[3h2v]] - hVCL C-terminal + raver1 RRM<br />
**[[3h2v]] - hVCL tail domain + raver1 RRM<br />
**[[4pr9]] - hVCL C-terminal + lipid<br />
**[[4pr9]] - hVCL tail domain + lipid<br />
**[[3jbi]] - hVCL tail domain + actin – Cryo-EM<br />
**[[3h2u]] – hVCL Vd1 + raver1 RRM <br />
**[[3h2u]] – hVCL Vd1 + raver1 RRM <br />
**[[2ibf]], [[2hsq]], [[2gww]] - hVCL Vd1 + SfVCL binding sites from ''Shigella flexneri''<br />
**[[2ibf]], [[2hsq]], [[2gww]] - hVCL Vd1 + SfVCL binding sites from ''Shigella flexneri''<br />
Line 30: Line 31:


**[[3myi]] – m-VCL tail domain <br />
**[[3myi]] – m-VCL tail domain <br />
**[[5l0f]], [[5l0i]], [[5l0 - hm-VCL tail domain (mutant)<br />
**[[5l0c]], [[5l0d]] - hm-VCL tail domain + lipid<br />
**[[5l0g]], [[5l0h]] - hm-VCL tail domain (mutant) + lipid<br />
**[[3jbk]] – hm-VCL tail domain + actin – Cryo-EM<br />
**[[3rf3]] - hm-VCL + invasin IPAA<br />  
**[[3rf3]] - hm-VCL + invasin IPAA<br />  
**[[3s90]] - hm-VCL head domain + mTalin-1 peptide<br />
**[[3s90]] - hm-VCL head domain + mTalin-1 peptide<br />

Revision as of 12:48, 13 December 2016

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].

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.

Chicken full-length metavinculin, 1st6

Drag the structure with the mouse to rotate

3D Structures of Vinculin3D Structures of Vinculin

Updated on 13-December-2016 {{#tree:id=OrganizedByTopic|openlevels=0|

  • Vinculin
    • 1tr2 – hVCL - human
    • 1qkr – hVCL tail domain
    • 3h2v - hVCL tail domain + raver1 RRM
    • 4pr9 - hVCL tail domain + lipid
    • 3jbi - hVCL tail domain + actin – Cryo-EM
    • 3h2u – hVCL Vd1 + raver1 RRM
    • 2ibf, 2hsq, 2gww - hVCL Vd1 + SfVCL binding sites from Shigella flexneri
    • 1ydi - hVCL Vd1+hActinin VBS
    • 1t01 - cVCL Vd1+mTalin VBS – chicken
    • 1syq, 1rkc, 1rke – hVCL Vd1+hTalin VBS
    • 3zdl – cVCL Vd1 + amyloid β precursor protein N terminal
  • Metavinculin
    • 3myi – m-VCL tail domain
    • 5l0f, 5l0i, [[5l0 - hm-VCL tail domain (mutant)
    • 5l0c, 5l0d - hm-VCL tail domain + lipid
    • 5l0g, 5l0h - hm-VCL tail domain (mutant) + lipid
    • 3jbk – hm-VCL tail domain + actin – Cryo-EM
    • 3rf3 - hm-VCL + invasin IPAA
    • 3s90 - hm-VCL head domain + mTalin-1 peptide
    • 4dj9 - hm-VCL head domain + hTalin-1 peptide
    • 3tj5 - hm-VCL head domain + Sca-family protein peptide
    • 3tj6 - hm-VCL head domain + protein Ps 120 peptide
    • 4ehp - hm-VCL head domain + catenin α-1 residues 277-382
    • 3vf0 – hm-VCL residues 856-1134 + ribonucleoprotein PTB-binding
    • 2gdc – cm-VCL Vd1+SfInvasin C-terminal
    • 1xwj - cm-VCL Vd1+cTalin VBS3
    • 1zvz, 1zw2, 1zw3, 1u6h - cm-VCL Vd1+cTalin rod
    • 1st6 – cm-VCL
    • 4e17, 4e18 - cm-VCL Vd1 + catenin α-1 VCL-binding domain

}}

ReferencesReferences

  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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Jaime Prilusky, Michal Harel