Structural insights into the function of human caveolin 1

被引：70

作者：

Spisni, E

Tomasi, V

Cestaro, A

Tosatto, SCE

机构：

[1] Univ Bologna, Dept Expt Biol, I-40126 Bologna, Italy

[2] Univ Padua, Dept Biol, I-35131 Padua, Italy

[3] Univ Padua, CRIBI Biotech Ctr, I-35131 Padua, Italy

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2005年 / 338卷 / 03期

关键词：

caveolin; 1; plasma membrane microdomains; structure prediction; transmembrane prediction; protein interactions;

D O I：

10.1016/j.bbrc.2005.10.099

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Caveolin-1 (Cav-1) is emerging as the central protein controlling caveolae formation, caveolae trafficking, and cellular signalling. In particular, it is known that Cav-1 interacts and modulates the activity of several signalling proteins through the so-called caveolin scaffolding domain. in this paper, We used a bioinformatics approach to assess the validity of some long-standing structural features of Cav-1. We could confirm the existence of a membrane spanning region of Cav-1 and highlight an interesting pattern of palmitoylated cysteine residues explaining the structural features of the Cav-1 C-terminal region. Moreover, the scaffolding domain is predicted to have a different structure than previously reported. (c) 2005 Elsevier Inc. All rights reserved.

引用

页码：1383 / 1390

页数：8

共 51 条

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Palmitoylation-dependent estrogen receptor α membrane localization:: Regulation by 17β-estradiol [J].