Cofilin weakly interacts with 14-3-3 and therefore can only indirectly participate in regulation of cell motility by small heat shock protein HspB6 (Hsp20)
- 作者：Maria V. Sudnitsyna ; Alim S. Seit-Nebi ; Nikolai B. Gusev ; NBGusev@mail.ru
- 关键词：14-3-3 ; Cofilin ; HspB6 ; Actin ; Phosphorylation
- 刊名：Archives of Biochemistry and Biophysics
- 出版年：2012
- 期刊代码：116_00039861
- 类别：ch
- 出版时间：May, 2012
- 卷：521
- 期：1-2
- 页码：62-70
- 文件大小：744 K
摘要
It has been previously reported that phosphorylated cofilin interacted with 14-3-3味 protein to generate a sub-micromolar Kd binary complex. Here we challenge this hypothesis by analyzing the direct association of recombinant cofilin with 14-3-3味 using different in vitro biochemical methods. Phosphorylated cofilin at high concentration binds to 14-3-3 immobilized on nitrocellulose, however no complex formation was detected by means of native gel electrophoresis or chemical crosslinking. Intact dimeric or mutant monomeric 14-3-3 was unable to form stable complexes with phosphorylated or unphosphorylated cofilin detected by size-exclusion chromatography. In co-sedimentation assay 14-3-3 did not affect interaction of cofilin with F-actin. The data of native gel electrophoresis indicate that 14-3-3 did not affect interaction of cofilin with G-actin. Thus, cofilin only weakly interacts with 14-3-3 and therefore cannot directly compete with phosphorylated small heat shock protein HspB6 for its binding to 14-3-3. It is hypothesized that phosphorylated HspB6 might affect interaction of 14-3-3 with protein phosphatases (and/or protein kinases) involved in dephosphorylation (or phosphorylation) of cofilin and by this means regulate cofilin-dependent reorganization of cytoskeleton.