Cloning and characterization of mCRIP2, a mouse LIM-only protein that interacts with PDZ domain IV of PTP-BL.

BACKGROUND: In the mouse submembranous protein tyrosine phosphatase PTP-BL five PDZ domains are present in between the N-terminal FERM domain, which directs the protein to the cell cortex, and the C-terminal catalytic phosphatase domain. To understand more on the physical role of PTP-BL in this microenvironment, we started to search ...
for PTP-BL PDZ domain-interacting proteins. RESULTS: Yeast two-hybrid screening for PTP-BL targets resulted in the identification of a novel mouse LIM-only protein termed CRIP2 that is highly homologous to rat ESP1 and human CRP2 sequences. Mouse CRIP2 has a predicted molecular weight of 23 kD and consists of two LIM domains spaced by 68 amino acids. The fourth PDZ domain of PTP-BL is responsible for the binding of CRIP2 protein. Both PTP-BL and CRIP2 mRNAs display a wide, overlapping tissue distribution. Western blot analysis revealed a more restricted expression pattern for CRIP2 with high expression in lung, heart and brain. CRIP2 protein is localized at cell cortical, actin-rich structures, which is concurrent with the subcellular localization of PTP-BL. CONCLUSIONS: The observed characteristics of the LIM domain-containing adaptor protein CRIP2 are consistent with a potential role of PTP-BL in the dynamics of the cortical actin cytoskeleton.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Cloning, Molecular, DNA, Complementary, Evolution, Molecular, Humans, Mice, Molecular Sequence Data, Nuclear Proteins, Precipitin Tests, Protein Binding, Protein Tyrosine Phosphatase, Non-Receptor Type 13, Protein Tyrosine Phosphatases, Proteins, Sequence Homology, Amino Acid, Subcellular Fractions, Two-Hybrid System Techniques
Genes Cells
Date: Jul. 01, 2003
Download Curated Data For This Publication
10175
Switch View:
  • Interactions 2