Vinculin: Difference between revisions

Revision as of 12:31, 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.

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.

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

Alexander Berchansky, Jaime Prilusky, Michal Harel

[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

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[2]

@@ Line 1: / Line 1: @@
 <StructureSection load='1st6' size='340' side='right' caption='Chicken full-length metavinculin, [[1st6]]' scene='' >
 == Function ==
-[[Vinculin|Vinculins]] (VCLs) are involved in adhesion by linking integrin molecules to the actin cytoskeleton. Its head domain (Vd1) can bind to [[Talin|talin]] or to [[Actinin|alpha-actinin]] at their respective VCL Binding Sites (VBS). A splice variant of vinculin is meta-vinculin (m-VCL). The protein raver1 RNA Recognition Motif (RRM) forms a complex with VCL or m-VCL.  <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.  '''Metavinculin''' is a splice version of VCL containing an extra ca. 70 amino acids in the C-terminal domain.
+[[Vinculin|Vinculins]] (VCLs) are involved in adhesion by linking integrin molecules to the actin cytoskeleton. Its head domain (Vd1) can bind to [[Talin|talin]] or to [[Actinin|alpha-actinin]] at their respective VCL Binding Sites (VBS)<ref>PMID:11152287</ref>.  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<ref>PMID:25496021</ref>.
 == Structural highlights ==