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MICAL, a novel CasL interacting molecule, associates with vimentin
Takahiro Suzuki1, Tetsuya Nakamoto, Seishi Ogawa
1Department of Hematology and Oncology, Graduate School of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8655, Japan.
The Journal of Biological Chemistry
|February 6, 2002
Summary
A novel protein, MICAL, interacts with CasL (p130Cas family) and vimentin, suggesting MICAL acts as a cytoskeletal regulator linking CasL to intermediate filaments in immune cells.
Area of Science:
- Cell Biology
- Molecular Biology
- Immunology
Background:
- CasL (p130Cas family) is crucial for immune responses, undergoing tyrosine phosphorylation upon integrin or T cell receptor stimulation.
- CasL possesses structural motifs like SH3 and substrate domains, mediating interactions with various molecules.
- Understanding CasL-mediated signal transduction requires identifying its interacting partners.
Purpose of the Study:
- To identify novel proteins interacting with the CasL SH3 domain.
- To elucidate the function of MICAL (Molecule Interacting with CasL) in cellular signaling and cytoskeletal organization.
Main Methods:
- Far Western screening to identify proteins binding to the CasL SH3 domain.
- Co-immunoprecipitation and colocalization studies to confirm MICAL-CasL interaction.
- Immunostaining to determine MICAL localization relative to vimentin.
Main Results:
- A novel 118 kDa protein, MICAL, was identified as a CasL-interacting molecule.
- MICAL binds CasL via its PPKPP sequence and associates with vimentin through its COOH-terminal region.
- MICAL colocalizes with CasL in the perinuclear area and with vimentin intermediate filaments.
Conclusions:
- MICAL connects the p130Cas signaling pathway to the intermediate filament cytoskeleton.
- MICAL functions as a potential cytoskeletal regulator, linking CasL to vimentin filaments.
- This interaction may play a significant role in cellular processes involving CasL and cytoskeletal dynamics.