Domain architecture of the atypical Arf-family GTPase Arl13b involved in cilia formation

被引:50
作者
Hori, Yuji [1 ]
Kobayashi, Tetsuo [1 ]
Kikko, Yorifumi [1 ]
Kontani, Kenji [1 ]
Katada, Toshiaki [1 ]
机构
[1] Univ Tokyo, Grad Sch Pharmaceut Sci, Dept Physiol Chem, Tokyo 1130033, Japan
基金
日本学术振兴会;
关键词
cilia; Arl13b; Arf; Arl; Ras; small GTPase; coiled-coil;
D O I
10.1016/j.bbrc.2008.06.001
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
Arl13b is an atypical Arf/Arl-family GTPase consisting of an extending large C-terminal region (C domain) and Arf-homologous GTP-binding motifs in the N terminus (N domain). Although Arl13b appears to be involved in cilia formation, its precise function and roles of the domains remain unknown. Here, we show the unique domain architecture of AM 3b by analyzing the relationship between its biochemical properties and cilia formation. Arl13b binds guanine nucleotides and specifically localizes to cilia. The ciliary localization of Arl13b requires both N and C domains but is independent of its guanine nucleotide-binding ability. Arl13b is capable of self-associating via N domain, and overexpression of N domain inhibits not only cilia formation but also the maintenance of pre-generated cilia. These findings suggest that N and C domains of Arl13b cooperatively regulate its ciliary localization and that N domain-dependent self-association of Arl13b may be important for its function in cilia biogenesis. (C) 2008 Elsevier Inc. All rights reserved.
引用
收藏
页码:119 / 124
页数:6
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