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First published online 28 July 2009
doi: 10.1242/jcs.046649

Journal of Cell Science 122, 2969-2979 (2009)
Published by The Company of Biologists 2009
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Research Article

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

Takashi Watanabe1,2,*, Jun Noritake1,3,*, Mai Kakeno1,4, Toshinori Matsui1, Takumi Harada1, Shujie Wang1, Norimichi Itoh1, Kazuhide Sato1, Kenji Matsuzawa1, Akihiro Iwamatsu5, Niels Galjart6 and Kozo Kaibuchi1,4,{ddagger}

1 Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, 65 Tsurumai, Showa, Nagoya, Aichi 466-8550, Japan
2 Institute for Advanced Research, Nagoya University, Furo, Chikusa, Nagoya, Aichi 464-8601, Japan
3 Department of Cell Physiology, Division of Membrane Physiology, National Institute for Physiological Sciences, Myodaiji, Okazaki, Aichi 444-8585, Japan
4 JST, CREST, 4-1-8 Honcho, Kawaguchi 332-0012, Japan
5 Protein Research Network, 1-13-5 Fukuura, Kanazawa, Yokohama, Kanagawa 236-0004, Japan
6 Department of Cell Biology and Genetics, Erasmus MC, 3000 DR Rotterdam, Netherlands

{ddagger} Author for correspondence (kaibuchi{at}med.nagoya-u.ac.jp)

Accepted 14 May 2009

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

Key words: GSK-3, IQGAP1, CLASP2, EB1, Microtubule


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© The Company of Biologists Ltd 2009