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A novel partner for the GTP-bound forms of rho and rac.

Authors :
Madaule P
Furuyashiki T
Reid T
Ishizaki T
Watanabe G
Morii N
Narumiya S
Source :
FEBS letters [FEBS Lett] 1995 Dec 18; Vol. 377 (2), pp. 243-8.
Publication Year :
1995

Abstract

Using the yeast two hybrid system and overlay assays we identified a putative rholrac effector, citron, which interacts with the GTP-bound forms of rho and rac1, but not with cdc42. Extensive homologies to known proteins were not observed. This 183 kDa protein contains a C6H2 zinc finger, a PH domain, and a long coiled-coil forming region including 4 leucine zippers and the rholrac binding site. We recently identified three others putative rho effectors characterized by a common rho binding motif. Citron does not share this motif and displays a distinctive protein organization, thus defining a separate class of rho partners.

Details

Language :
English
ISSN :
0014-5793
Volume :
377
Issue :
2
Database :
MEDLINE
Journal :
FEBS letters
Publication Type :
Academic Journal
Accession number :
8543060
Full Text :
https://doi.org/10.1016/0014-5793(95)01351-2