Caveolin regulates microtubule polymerization in the vascular smooth muscle cells

被引:20
|
作者
Kawabe, J [1 ]
Okumura, S
Nathanson, MA
Hasebe, N
Ishikawa, Y
机构
[1] Univ Med & Dent New Jersey, Dept Cell Biol & Mol Med, Cardiovasc Res Inst, Newark, NJ 07103 USA
[2] Univ Med & Dent New Jersey, Dept Med Cardiol, Newark, NJ 07103 USA
[3] Asahikawa Med Coll, Dept Med, Asahikawa, Hokkaido 0788510, Japan
[4] Yokohama City Univ, Grad Sch Med, Cardiovasc Res Inst, Yokohama, Kanagawa 2360004, Japan
关键词
scaffolding domain peptide; Stathmin; depolymerization;
D O I
10.1016/j.bbrc.2006.01.125
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 and caveolin have common properties in intracellular trafficking and the regulation of cellular growth. Overexpression of caveolin in vascular smooth muscle cells increased the polymer form of microtubule without changing in the total amount of tubulin, and downregulation of caveolin decreased the polymer form of microtubule. Fractionation of cellular proteins followed by immunodetection as well as immunostaining of caveolin and microtubule revealed that caveolin and a portion of microtubule were co-localized in caveolar fractions. A caveolin scaffolding domain peptide, which mimics caveolin function, did not alter the polymerization of microtubule in vitro, but dramatically inhibited the depolymerization of microtubule induced by stathmin, a microtubule destabilizing protein, which was also found in caveolar fractions. Accordingly, it is most likely that caveolin increased the polymer form of microtubule through the inhibition of a microtubule destabilizer, stathmin, suggesting a novel role of caveolin in regulating cellular network and trafficking. (c) 2006 Elsevier Inc. All rights reserved.
引用
收藏
页码:164 / 169
页数:6
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