MICAL, a novel CasL interacting molecule, associates with vimentin.

CasL/HEF1 belongs to the p130(Cas) family. It is tyrosine-phosphorylated following beta(1) integrin and/or T cell receptor stimulation and is thus considered to be important for immunological reactions. CasL has several structural motifs such as an SH3 domain and a substrate domain and interacts with many molecules through these motifs. To ...
obtain more insights on the CasL-mediated signal transduction, we sought proteins that interact with the CasL SH3 domain by far Western screening, and we identified a novel human molecule, MICAL (a Molecule Interacting with CasL). MICAL is a protein of 118 kDa and is expressed in the thymus, lung, spleen, kidney, testis, and hematopoietic cells. MICAL has a calponin homology domain, a LIM domain, a putative leucine zipper motif, and a proline-rich PPKPP sequence. MICAL associates with CasL through this PPKPP sequence. MICAL is a cytoplasmic protein and colocalizes with CasL at the perinuclear area. Through the COOH-terminal region, MICAL also associates with vimentin that is a major component of intermediate filaments. Immunostaining revealed that MICAL localizes along with vimentin intermediate filaments. These results suggest that MICAL may be a cytoskeletal regulator that connects CasL to intermediate filaments.
Mesh Terms:
Amino Acid Sequence, Base Sequence, Cell Line, Cytoskeletal Proteins, DNA, Complementary, Intracellular Signaling Peptides and Proteins, Microscopy, Fluorescence, Molecular Sequence Data, Plasmids, Protein Binding, RNA, Messenger, Vimentin
J. Biol. Chem.
Date: Apr. 26, 2002
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