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

FEBS Lett. 1995 Dec 18;377(2):243-8. doi: 10.1016/0014-5793(95)01351-2.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Binding Sites
  • Cell Cycle Proteins*
  • Cell Line
  • DNA, Complementary
  • GTP-Binding Proteins / metabolism*
  • Guanosine Triphosphate / metabolism*
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins / metabolism
  • Mice
  • Molecular Sequence Data
  • Protein Binding
  • Protein Serine-Threonine Kinases*
  • Proteins / chemistry
  • Proteins / metabolism*
  • Signal Transduction
  • rac GTP-Binding Proteins
  • ras Proteins
  • rho GTP-Binding Proteins*
  • rhoA GTP-Binding Protein
  • rhoB GTP-Binding Protein
  • rhoC GTP-Binding Protein

Substances

  • Cell Cycle Proteins
  • DNA, Complementary
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Proteins
  • Guanosine Triphosphate
  • citron-kinase
  • Protein Serine-Threonine Kinases
  • GTP-Binding Proteins
  • Rhoc protein, mouse
  • rac GTP-Binding Proteins
  • ras Proteins
  • rho GTP-Binding Proteins
  • rhoA GTP-Binding Protein
  • rhoB GTP-Binding Protein
  • rhoC GTP-Binding Protein

Associated data

  • GENBANK/U39904