Plath K, Engel K, Schwedersky G, Gaestel M
Max-Delbrück-Centrum for Molecular Medicine, Berlin, Germany.
Biochem Biophys Res Commun. 1994 Sep 15;203(2):1188-94. doi: 10.1006/bbrc.1994.2308.
The primary structure of mouse MAP kinase-activated protein (MAPKAP) kinase 2 contains a proline-rich N-terminal region which might function as a src-homology 3 (SH3) domain-binding motif in vivo. To demonstrate the ability of this region to bind SH3 domains, we analyzed the interaction of the SH3 domain of the protein tyrosine kinase c-abl with MAPKAP kinase 2. It is demonstrated, that the proline-rich region specifically binds c-abl-SH3 domain in vitro. Furthermore, it is shown, that deletion of this proline-rich region does not significantly influence the substrate binding properties of the enzyme when analyzed with the substrate small heat shock protein Hsp25. The data suggest that the proline-rich region of MAPKAP kinase 2 could interact with proteins containing SH3-domains also in vivo regulating its cellular localization and/or modulating its enzymatic properties.
小鼠丝裂原活化蛋白（MAP）激酶激活蛋白激酶2的一级结构包含一个富含脯氨酸的N端区域，该区域在体内可能作为src同源3（SH3）结构域结合基序发挥作用。为了证明该区域结合SH3结构域的能力，我们分析了蛋白酪氨酸激酶c-abl的SH3结构域与MAPKAP激酶2的相互作用。结果表明，富含脯氨酸的区域在体外能特异性结合c-abl-SH3结构域。此外，研究表明，在用底物小分子热休克蛋白Hsp25进行分析时，删除该富含脯氨酸的区域对该酶的底物结合特性没有显著影响。这些数据表明，MAPKAP激酶2的富含脯氨酸区域在体内也可能与含SH3结构域的蛋白质相互作用，从而调节其细胞定位和/或调节其酶活性。
