Vasodilator-stimulated phosphoprotein: Difference between revisions

Revision as of 13:28, 21 March 2017

Function

Vasodilator-stimulated phosphoprotein (VASP) belongs to the Ena-VASP family. It binds proteins with E/DFPPPPXD/E motif and targets them to focal adhesion cell membranes. VASP is an actin- and profilin-binding protein^[1]. VASP is associated with filament formation and promotes elongation.

VASP protects the actin barb edge against capping and increases the rate of actin polymerization in the presence of capping protein. VASP is a homotetramer. For more details see Group:MUZIC:Mena_VASP.

Relevance

VASP restricts the spread of Shigella which causes diarrhoreal disease^[2].

Structural highlights

VAS binds actin with a poly-Pro site^[3].

Human VASP (dark olive) complex with α-actin (cyan), profilin-1 (green), ATP and Ca+2 ion (green), 2pbd

Drag the structure with the mouse to rotate

3D structure of vasodilator-stimulated phosphoprotein3D structure of vasodilator-stimulated phosphoprotein

Updated on 21-March-2017

1egx – hVASP EVH1 domain – human – NMR
1usd, 1use - hVASP tetramerization domain
2pav, 2pbd, 3chw – hVASP + actin + profilin-1

ReferencesReferences

↑ Wentworth JK, Pula G, Poole AW. Vasodilator-stimulated phosphoprotein (VASP) is phosphorylated on Ser157 by protein kinase C-dependent and -independent mechanisms in thrombin-stimulated human platelets. Biochem J. 2006 Jan 15;393(Pt 2):555-64. PMID:16197368 doi:http://dx.doi.org/BJ20050796
↑ Lee SY, Gertler FB, Goldberg MB. Vasodilator-stimulated phosphoprotein restricts cell-to-cell spread of Shigella flexneri at the cell periphery. Microbiology. 2015 Nov;161(11):2149-60. doi: 10.1099/mic.0.000173. Epub 2015 Sep , 9. PMID:26358985 doi:http://dx.doi.org/10.1099/mic.0.000173
↑ Ferron F, Rebowski G, Lee SH, Dominguez R. Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J. 2007 Oct 31;26(21):4597-606. Epub 2007 Oct 4. PMID:17914456

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

Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] Wentworth JK, Pula G, Poole AW. Vasodilator-stimulated phosphoprotein (VASP) is phosphorylated on Ser157 by protein kinase C-dependent and -independent mechanisms in thrombin-stimulated human platelets. Biochem J. 2006 Jan 15;393(Pt 2):555-64. PMID:16197368 doi:http://dx.doi.org/BJ20050796

[2] Lee SY, Gertler FB, Goldberg MB. Vasodilator-stimulated phosphoprotein restricts cell-to-cell spread of Shigella flexneri at the cell periphery. Microbiology. 2015 Nov;161(11):2149-60. doi: 10.1099/mic.0.000173. Epub 2015 Sep , 9. PMID:26358985 doi:http://dx.doi.org/10.1099/mic.0.000173

[3] Ferron F, Rebowski G, Lee SH, Dominguez R. Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J. 2007 Oct 31;26(21):4597-606. Epub 2007 Oct 4. PMID:17914456

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-<StructureSection load='2pbd' size='340' side='right' caption='Human VASP (dark olive) complex with α-actin (grey), profilin-1 (green), ATP (stick model) and Ca+2 ion (green), [[2pbd]]' scene='' >
+<StructureSection load='2pbd' size='400' side='right' caption='Human VASP (dark olive) complex with α-actin (cyan), profilin-1 (green), ATP and Ca+2 ion (green), [[2pbd]]' scene='50/508423/Cv/1' pspeed='8'>
 == Function ==
 '''Vasodilator-stimulated phosphoprotein''' (VASP) belongs to the Ena-VASP family.  It binds proteins with E/DFPPPPXD/E motif and targets them to focal adhesion cell membranes.  VASP is an actin- and profilin-binding protein<ref>PMID:16197368</ref>.  VASP is associated with filament formation and promotes elongation.