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Cloning and characterization of mCRIP2, a mouse LIM‐only protein that interacts with PDZ domain IV of PTP‐BL
Author(s) -
Van Ham Marco,
Croes Huib,
Schepens Jan,
Fransen Jack,
Wieringa Bé,
Hendriks Wiljan
Publication year - 2003
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1046/j.1365-2443.2003.00660.x
Subject(s) - pdz domain , biology , protein tyrosine phosphatase , microbiology and biotechnology , lim domain , signal transducing adaptor protein , phosphatase , actin cytoskeleton , cytoskeleton , biochemistry , phosphorylation , cell , gene , transcription factor , zinc finger
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.