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J. Biol. Chem., Vol. 281, Issue 48, 36477-36481, December 1, 2006

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Minireview

The VASP-Spred-Sprouty Domain Puzzle^*

Karin Bundschu¹, Ulrich Walter, and Kai Schuh^¶

From the Abteilung Biochemie und Molekulare Biologie, Universität Ulm, 89081 Ulm, Institut für Klinische Biochemie und Pathobiochemie, Universität Würzburg, 97080 Würzburg, and ^¶Physiologisches Institut, Universität Würzburg, 97070 Würzburg, Germany

Sprouty-related proteins with an EVH1 domain (Spreds) belong to a new protein family harboring a conserved N-terminal EVH1 domain, which is related to the VASP (vasodilator-stimulated phosphoprotein) EVH1 domain (Enabled/VASP homology 1 domain) and a C-terminal Sprouty-related domain, typical for Sprouty proteins. Spreds were, like Sproutys, initially discovered as inhibitors of the Ras/MAPK pathway, and the SPR (Sprouty-related) domains of both protein families seem to be very important for many protein interactions and cellular processes. VASP was initially characterized as a proline-rich substrate of protein kinases A and G in human platelets and later shown to be a scaffold protein, regulating both signal transduction pathways and the actin filament system. The VASP-EVH1 domain is known to bind specifically to a FP₄ binding motif, which is, for example, present in the focal adhesion proteins vinculin and zyxin. In this review we give a structural and functional overview on these three protein families and ask whether nature plays a modular protein domain puzzle with stable exchangeable elements or if these closely related domains have various functions when pasted in a different protein context.

^* This minireview will be reprinted in the 2006 Minireview Compendium, which will be available in January, 2007. This work was supported by the Ministerium für Wissenschaft, Forschung und Kunst, Baden-Württemberg, Germany ("Stipendium der Universität Ulm" (to K. B.) and by the DFG.

¹ To whom correspondence should be addressed. Tel.: 49-731-50-23281; Fax: 49-731-50-23277; E-mail: karin.bundschu{at}gmx.de.

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