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A novel partner for the GTP-bound forms of rho and rac.
- 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.
- Subjects :
- Amino Acid Sequence
Animals
Base Sequence
Binding Sites
Cell Line
DNA, Complementary
Intracellular Signaling Peptides and Proteins
Membrane Proteins metabolism
Mice
Molecular Sequence Data
Protein Binding
Proteins chemistry
Signal Transduction
rac GTP-Binding Proteins
ras Proteins
rhoA GTP-Binding Protein
rhoB GTP-Binding Protein
rhoC GTP-Binding Protein
Cell Cycle Proteins
GTP-Binding Proteins metabolism
Guanosine Triphosphate metabolism
Protein Serine-Threonine Kinases
Proteins metabolism
rho GTP-Binding Proteins
Subjects
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