共 22 条
Microtubule binding proteins CLIP-170, EB1, and p150Glued form distinct plus-end complexes
被引:41
作者:

Ligon, LA
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机构:
Univ Penn, Dept Physiol, Philadelphia, PA 19104 USA Univ Penn, Dept Physiol, Philadelphia, PA 19104 USA

Shelly, SS
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h-index: 0
机构:
Univ Penn, Dept Physiol, Philadelphia, PA 19104 USA Univ Penn, Dept Physiol, Philadelphia, PA 19104 USA

Tokito, MK
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机构:
Univ Penn, Dept Physiol, Philadelphia, PA 19104 USA Univ Penn, Dept Physiol, Philadelphia, PA 19104 USA

Holzbaur, ELF
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h-index: 0
机构:
Univ Penn, Dept Physiol, Philadelphia, PA 19104 USA Univ Penn, Dept Physiol, Philadelphia, PA 19104 USA
机构:
[1] Univ Penn, Dept Physiol, Philadelphia, PA 19104 USA
来源:
FEBS LETTERS
|
2006年
/
580卷
/
05期
关键词:
microtubule-binding proteins;
EBI;
CLIP-170;
p150(Glued);
D O I:
10.1016/j.febslet.2006.01.050
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Microtubule plus-end proteins CLIP-170 and EB1 dynamically track the tips of growing microtubules in vivo. Here we examine the association of these proteins with microtubules in vitro. CLIP-170 binds tubulin dimers and co-assembles into growing microtubules. EB1 binds tubulin dimers more weakly, so no co-assembly is observed. However, EB1 binds to CLIP170, and forms a co-complex with CLIP-170 and tubulin that is recruited to growing microtubule plus ends. The interaction between CLIP-170 and EB1 is competitively inhibited by the related CAP-Gly protein p150(Glued), which also localizes to microtubule plus ends in vivo. Based on these observations, we propose a model in which the formation of distinct plus-end complexes may differentially affect microtubule dynamics in vivo. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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页码:1327 / 1332
页数:6
相关论文
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