TY - JOUR
T1 - CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics at the cell cortex
AU - Mimori-Kiyosue, Yuko
AU - Grigoriev, Ilya
AU - Lansbergen, Gideon
AU - Sasaki, Hiroyuki
AU - Matsui, Chiyuki
AU - Severin, Fedor
AU - Galjart, Niels
AU - Grosveld, Frank
AU - Vorobjev, Ivan
AU - Tsukita, Shoichiro
AU - Akhmanova, Anna
N1 - Copyright:
Copyright 2008 Elsevier B.V., All rights reserved.
PY - 2005/1/3
Y1 - 2005/1/3
N2 - 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.
AB - 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.
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U2 - 10.1083/jcb.200405094
DO - 10.1083/jcb.200405094
M3 - Article
C2 - 15631994
AN - SCOPUS:19944429410
VL - 168
SP - 141
EP - 153
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 1
ER -