Phosphorylation of CLASP2 by GSK-3β regulates its interaction with IQGAP1, EB1 and microtubules

• DOI: 10.1242/jcs.046649
• Publication Date: 2009-07-29T01:39:32Z
• Authors: Takashi Watanabe; Jun Noritake; Mai Kakeno; Toshinori Matsui; Takumi Harada; Shujie Wang; Norimichi Itoh; Kazuhide Sato; Kenji Matsuzawa; Akihiro Iwamatsu; Niels Galjart; Kozo Kaibuchi
• Keywords: IQGAP1

Polarised cell migration is required for various behaviours and functions. Actin microtubules are coupled structurally distributed asymmetrically along the front-rear axis of migrating cells. CLIP-associating proteins (CLASPs) accumulate near ends at front cells to control microtubule dynamics cytoskeletal coupling. Regional inhibition GSK-3beta responsible this asymmetric distribution CLASPs. However, it not known how regulates activity CLASPs linkage between actin microtubules. Here we identified IQGAP1, an actin-binding protein, as a novel CLASP-binding protein. directly phosphorylates CLASP2 Ser533 Ser537 within region IQGAP1 binding. Phosphorylation results in dissociation from EB1 At leading edges fibroblasts, partially colocalises with IQGAP1. Expression active abrogates on microtubules, but that nonphosphorylatable mutant. The phosphorylated does edges. Thus, phosphorylation by appears regional filaments through migration.