Group:MUZIC:Mena VASP
From Proteopedia
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== Introduction == | == Introduction == | ||
| - | 'Ena/VASP protein family contributes cell motility and cell adhesion through the regulation of actin dynamics and consists of three members in mammalian: Vasodilator-stimulated phosphoprotein (VASP), Mena (mammalian enabled), and the Ena-VASP-like protein Evl. They contain three domains: N-terminal Ena/Vasp like homology domain 1 (EVH1) with an optimal core consensus motif of “FPPPP”, central proline-rich region and C-terminal EVH2 domain. Ena/VASP proteins localize in the hot spots of actin reassembly such as tips of lamellipodia and filopodia. | + | 'Ena/VASP protein family contributes cell motility and cell adhesion through the regulation of actin dynamics and consists of three members in mammalian: Vasodilator-stimulated phosphoprotein (VASP), Mena (mammalian enabled), and the Ena-VASP-like protein Evl. They contain three domains: N-terminal Ena/Vasp like homology domain 1 (EVH1) with an optimal core consensus motif of “FPPPP”, central proline-rich region and C-terminal EVH2 domain. Ena/VASP proteins associate with actin filaments and localize in the hot spots of actin reassembly such as tips of lamellipodia and filopodia. |
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== Function and interaction == | == Function and interaction == | ||
| - | EVH1 domain of Mena/VASP binds to the cytoskeleton proteins containing FPPPP motif, such as vinculin <ref>PMID:8980130</ref>, lamellipodin <ref>PMID:15469845</ref>, zyxin <ref>PMID:10801818</ref>, palladin <ref>PMID:14983521</ref> and Xin <ref>PMID:16631741</ref>. The Pro-rich region of Mena/VASP binds profilin and the SH3 and WW domains of various signaling and scaffolding proteins. EVH2 domain comprises F- ang G-Actin binding sites and C-terminal coiled coil region, also known as tetramerization domain <ref>PMID:10438535</ref>. It is suggested that Mena/VASP bind to the barbed end of actin filaments and prevent their capping by CapZ <ref>PMID:10438535</ref>. | + | EVH1 domain of Mena/VASP binds to the cytoskeleton proteins containing FPPPP motif, such as vinculin <ref>PMID:8980130</ref>, lamellipodin <ref>PMID:15469845</ref>, zyxin <ref>PMID:10801818</ref>, palladin <ref>PMID:14983521</ref> and Xin <ref>PMID:16631741</ref>. The Pro-rich region of Mena/VASP binds profilin and the SH3 and WW domains of various signaling and scaffolding proteins. EVH2 domain comprises F- ang G-Actin binding sites and C-terminal coiled coil region, also known as tetramerization domain <ref>PMID:10438535</ref>. It was shown recently that Mena binds with fibronectin receptor α5β1 integrin via “LERER" motif <ref>PMID:22908313</ref>. It is suggested that Mena/VASP bind to the barbed end of actin filaments and prevent their capping by CapZ <ref>PMID:10438535</ref>. Regulation of VASP protein activity occurs through phosphorylation at Ser-157, Ser-239, and Thr-278. |
Revision as of 20:05, 3 October 2012
Mena/VASP
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