CPAP interacts with 14-3-3 in a cell cycle-dependent manner

Chen, CY; Olayioye, MA; Lindeman, GJ; Tang, TK

Author(s): Chen, CY; Olayioye, MA; Lindeman, GJ; Tang, TK;
Details: Publication Year 2006-04-21,Volume 342,Issue #4,Page 1203-1210
Journal Title: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Publication Type: Journal Article
Abstract: We have previously reported that CPAP (Centrosomal Protein 4.1-Associated Protein) carries a novel microtubule-destabilizing motif that may regulate microtubule dynamics at the centrosome. In this study, we searched for conserved sequence motifs in CPAP and identified two classical 14-3-3 binding sites. The interaction between CPAP and 14-3-3 was demonstrated by both yeast two-hybrid and co-immunoprecipitation experiments. Further analyses revealed that the 14-3-3 binding motif is located within the C-terminal domain of CPAP. Alkaline phosphatase treatment disrupted CPAP binding to 14-3-3, Suggesting that phosphorylation is required for the interaction. Mutation of serine 1109 to alanine (S1 109A) in the 14-3-3 binding motif completely abolished the association of CPAP with 14-3-3. Taking together, these results imply that phosphorylation of CPAP on serine 1109 is required for 14-3-3 binding. Furthermore, we observed that the interaction between CPAP and 14-3-3 was significantly reduced in mitotic cells. suggesting that 14-3-3 binding to CPAP is regulated during cell cycle progression. In Summary, Our results show a direct interaction between CPAP and 14-3-3, and this interaction appears to be phosphorylation and cell cycle dependent. (c) 2006 Elsevier Inc. All rights reserved.
Publisher: ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords: PROTEIN-BINDING; CENTROSOME; PHOSPHORYLATION; ASSOCIATION; KINASE; CDC25C; WEE1
Publisher's Version: https://doi.org/10.1016/j.bbrc.2006.02.089
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2006-04-21 12:00:00