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

Abstract：

: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 Arl13b 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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Hori Y,Kobayashi T,Kikko Y,Kontani K,Katada T

doi

10.1016/j.bbrc.2008.06.001

subject

Has Abstract

pub_date

2008-08-15 00:00:00

pages

119-24

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(08)01122-4

journal_volume

373

pub_type

杂志文章

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