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Originally published In Press as doi:10.1074/jbc.M111842200 on February 4, 2002

J. Biol. Chem., Vol. 277, Issue 17, 14933-14941, April 26, 2002
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MICAL, a Novel CasL Interacting Molecule, Associates with Vimentin*

Takahiro SuzukiDagger , Tetsuya NakamotoDagger , Seishi OgawaDagger , Sachiko SeoDagger , Tomoko MatsumuraDagger , Kouichi Tachibana§, Chikao Morimoto, and Hisamaru HiraiDagger ||

From the Dagger  Department of Hematology and Oncology, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8655, the § Laboratory of Gene Function Analysis, Institute of Molecular and Cell Biology, National Institute of Advanced Industrial Science and Technology, Central-2 OSL-C2, 1-1-1 Umezono, Tsukuba, Ibaraki 305-8568, and the  Department of Clinical Immunology and AIDS Research Center, Institute of Medical Science, University of Tokyo, 4-6-1 Shiroganedai, Minato-ku, Tokyo 108-8639, Japan

CasL/HEF1 belongs to the p130Cas 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.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AB048948.

|| To whom correspondence should be addressed: Dept. of Hematology and Oncology, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8655, Japan. Tel.: 81-3-5800-6421; Fax: 81-3-5689-7286; E-mail: hhirai-tky@umin.ac.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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