Identification of cofilin and LIM-domain-containing protein kinase 1 as novel 
interaction partners of 14-3-3 zeta

Birkenfeld, J.; Betz, H.; Roth, D.

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Identification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3 zeta

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Birkenfeld, J.
Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society;

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Betz, H.
Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society;

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Roth, D.
Neurochemistry Department, Max Planck Institute for Brain Research, Max Planck Society;

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引用

Birkenfeld, J., Betz, H., & Roth, D. (2003). Identification of cofilin and LIM-domain-containing protein kinase 1 as novel interaction partners of 14-3-3 zeta. Biochemical Journal, 369, 45-54.

引用: https://hdl.handle.net/11858/00-001M-0000-002E-1EFA-4

要旨

Proteins of the 14-3-3 family have been implicated in various physiological processes, and are thought to function as adaptors in various signal transduction pathways. In addition, 14-3-3 proteins may contribute to the reorganization of the actin cytoskeleton by interacting with as yet unidentified actin-binding proteins. Here we show that the 14-3-3 isoform interacts with both the actin-depolymerizing factor cofilin and its regulatory kinase, LIM (Lin-11/Isl-1/Mec-3)-domain- containing protein kinase 1 (LIMK1). In both yeast two-hybrid assays and glutathione S-transferase pull-down experiments, these proteins bound efficiently to 14-3-3zeta. Deletion analysis revealed consensus 14-3-3 binding sites on both cofilin and LIMK1. Furthermore, the C-terminal region of 14-3- zeta inhibited the binding of cofilin to actin in co- sedimentation experiments. Upon co-transfeefion into COS-7 cells, 14-3-zeta-specific immunoreactivity was redistributed into characteristic LIMK1-induced actin aggregations. Our data are consistent with 14-3-3-protein-induced changes to the actin cytoskeleton resulting from interactions with cofilin and/or LIMK1.