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

P Madaule, T Furuyashiki, T Reid, T Ishizaki… - FEBS …, 1995 - Wiley Online Library
P Madaule, T Furuyashiki, T Reid, T Ishizaki, G Watanabe, N Morii, S Narumiya
FEBS letters, 1995Wiley Online Library
Using the yeast two hybrid system and overlay assays we identified a putative rho/rac
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 rho/rac binding site. We recently identified three others putative rho
effectors characterized by a common rho binding motif. Citron does not share this motif and …
Using the yeast two hybrid system and overlay assays we identified a putative rho/rac 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 rho/rac 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.
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