Vinculin: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<scene name='Sandbox_27/Role_i997_vinculin_head-tail_1/1'>Vinculin Autoinhibition</scene> is achieved through a high affinity intramolecular interaction between tail (orange) and head (aqua) domains ([[1st6]]). Energetically, I997 is key to maintaining this autoinhibition.
<scene name='Sandbox_27/Role_i997_vinculin_head-tail_1/1'>Vinculin Autoinhibition</scene> is achieved through a high affinity intramolecular interaction between tail (orange) and head (aqua) domains ([[1st6]]). Energetically, I997 is key to maintaining this autoinhibition.
</StructureSection>
 
== 3D Structures of Vinculin ==
== 3D Structures of Vinculin ==
[[Vinculin 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
*Vinculin; Domains - head  140-327; tail 878-1066
**[[1tr2]], [[6fuy]] – hVCL - human<br />
**[[3h2u]] – hVCL head domain + raver1 RRM <br />
**[[2ibf]], [[2hsq]], [[2gww]] - hVCL head domain + SfVCL binding sites from ''Shigella flexneri''<br />
**[[1ydi]] - hVCL head domain +hActinin VBS<br />
**[[1syq]], [[1rkc]], [[1rke]] – hVCL head domain +hTalin VBS<br />
**[[1qkr]] – hVCL tail domain<br />
**[[3h2v]] - hVCL tail domain + raver1 RRM<br />
**[[4pr9]] - hVCL tail domain + lipid<br />
**[[3jbi]] - hVCL tail domain + actin – Cryo-EM<br />
**[[6nr7]] - cVCL – chicken<br />
**[[1t01]] - cVCL head domain +mTalin VBS<br />
**[[3zdl]] – cVCL head domain + amyloid β precursor protein N terminal<br />
*Metavinculin; Domains - head 1-256; tail 959-1134
**[[7ktt]], [[7ktu]], [[7ktv]], [[7ktw]] – hVCL – Cryo-EM<br />
**[[6upw]] – hVCL + actin + ADP – Cryo-EM<br />
**[[6fuy]] - hVCL <br />
**[[3rf3]] - hVCL head domain + invasin IPAA<br />
**[[3s90]] - hVCL head domain + mTalin-1 peptide<br />
**[[4dj9]] - hVCL head domain + hTalin-1 peptide <br />
**[[6fq4]] - hVCL head domain + TARP peptide <br />
**[[3tj5]] - hVCL head domain + Sca-family protein peptide<br />
**[[3tj6]] - hVCL head domain + protein Ps 120 peptide<br />
**[[4ehp]], [[5y04]] - hVCL head domain + catenin α-1 residues 277-382<br />
**[[3myi]] – hVCL tail domain <br />
**[[5l0f]], [[5l0i]], [[5l0j]] - hVCL tail domain (mutant)<br />
**[[5l0c]], [[5l0d]] - hVCL tail domain + lipid<br />
**[[5l0g]], [[5l0h]] - hVCL tail domain (mutant) + lipid<br />
**[[3jbk]] – hVCL tail domain + actin – Cryo-EM<br />
**[[6upw]] - mVCL head domain + catenin α-1<br />
**[[3vf0]] – hVCL tail domain + ribonucleoprotein PTB-binding<br />
**[[1st6]] – cVCL<br />
**[[2gdc]] – cVCL head domain +SfInvasin C-terminal <br />
**[[1xwj]] - cVCL head domain +cTalin VBS3<br />
**[[1zvz]], [[1zw2]], [[1zw3]], [[1u6h]] - cVCL head domain +cTalin rod<br />
**[[6fq4]] – cVCL head domain + TARP-VBS1<br />
**[[4e17]], [[4e18]] - cVCL head domain + catenin α-1 VCL-binding domain
}}
==References==
==References==
<references />
<references />
</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]


*Created with the participation of [[User:Susan Craig|Susan Craig]].
*Created with the participation of [[User:Susan Craig|Susan Craig]].

Latest revision as of 11:07, 19 March 2024

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

Vinculin 3D structures

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

Chicken full-length metavinculin, 1st6

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

Alexander Berchansky, Jaime Prilusky, Michal Harel
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