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Published 3 January 2005. doi:10.1083/jcb.200405094
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 1, 141-153
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Article

CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics at the cell cortex



Yuko Mimori-Kiyosue1, Ilya Grigoriev2,3, Gideon Lansbergen4, Hiroyuki Sasaki1,5, Chiyuki Matsui1, Fedor Severin6, Niels Galjart4, Frank Grosveld4, Ivan Vorobjev3, Shoichiro Tsukita7,8, and Anna Akhmanova4

1 KAN Research Institute, Kyoto Research Park, Shimogyo-ku, Kyoto 600-8815, Japan
2 Department of Cell Biology and Histology, A.N. Belozersky Institute, Moscow State University, Vorobjevi Gory, Moscow, 119992, Russia
3 Laboratory of Cell Motility, A.N. Belozersky Institute, Moscow State University, Vorobjevi Gory, Moscow, 119992, Russia
4 MGC Department of Cell Biology and Genetics, Erasmus Medical Center, 3000 DR Rotterdam, Netherlands
5 Institute of DNA Medicine, Jikei University School of Medicine, Minato-ku, Tokyo 105-8461, Japan
6 BIOTEC, TU Dresden, Proteomics and Cellular Machines, Tatzberg 47-51, 01307 Dresden, Germany
7 Department of Cell Biology, Faculty of Medicine, Kyoto University, Sakyo-ku, Kyoto 606-8315, Japan
8 Solution Oriented Research for Science and Technology, Japan Science and Technology Corporation, Sakyo-ku, Kyoto 606-8501, Japan

Correspondence to Anna Akhmanova: anna.akhmanova{at}chello.nl

CLIP-associating protein (CLASP) 1 and CLASP2 are mammalian microtubule (MT) plus-end binding proteins, which associate with CLIP-170 and CLIP-115. Using RNA interference in HeLa cells, we show that the two CLASPs play redundant roles in regulating the density, length distribution and stability of interphase MTs. In HeLa cells, both CLASPs concentrate on the distal MT ends in a narrow region at the cell margin. CLASPs stabilize MTs by promoting pauses and restricting MT growth and shortening episodes to this peripheral cell region. We demonstrate that the middle part of CLASPs binds directly to EB1 and to MTs. Furthermore, we show that the association of CLASP2 with the cell cortex is MT independent and relies on its COOH-terminal domain. Both EB1- and cortex-binding domains of CLASP are required to promote MT stability. We propose that CLASPs can mediate interactions between MT plus ends and the cell cortex and act as local rescue factors, possibly through forming a complex with EB1 at MT tips.

Abbreviations used in this paper: APC, adenomatous polyposis coli; CLASP, CLIP-associating protein; HIS, 6x histidine; mRFP, monomeric RFP; MT, microtubule; siRNA, small interfering RNA; +TIPs, plus-end tracking proteins; TIRF, total internal reflection fluorescence.


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