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Originally published In Press as doi:10.1074/jbc.M212113200 on December 13, 2002

J. Biol. Chem., Vol. 278, Issue 10, 8452-8459, March 7, 2003
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Mouse MIM, a Tissue-specific Regulator of Cytoskeletal Dynamics, Interacts with ATP-Actin Monomers through Its C-terminal WH2 Domain*

Pieta K. MattilaDagger , Marjo Salminen§, Takashi Yamashiro§, and Pekka LappalainenDagger

From the Programs in Dagger  Cellular Biotechnology and § Developmental Biology, Institute of Biotechnology, P. O. Box 56, University of Helsinki, Helsinki 00014, Finland

The WH2 (WASP homology domain-2) is a small actin monomer-binding motif and is found in many proteins that regulate the actin cytoskeleton, including the beta -thymosins, ciboulot, WASP, and verprolin/WIP (WASP-interacting protein). In sequence database searches we identified a novel mouse protein containing a WH2 domain in its C-terminal region. This mouse gene also shows strong sequence homology to human MIM (Missing in Metastasis), a cDNA fragment that is present in non-metastatic but absent in metastatic bladder cancer cell lines. Northern blot and in situ hybridizations show that MIM is strongly expressed in the developing neurons and skeletal and cardiac muscles in mouse embryos. In adult mice, the strongest expression of MIM mRNA is in liver, outer layers of the kidney, and in the Purkinje cells of the brain. Recombinant MIM protein interacts with actin monomers and inhibits actin filament nucleation in vitro. However, the MIM/ATP-G-actin complex can participate in actin filament assembly at the barbed end. MIM binds ATP-G-actin with a higher affinity (KD = 0.06 µM) than ADP-G-actin (KD = 0.3 µM) and inhibits the nucleotide exchange on actin monomers. Site-directed mutagenesis demonstrates that the actin monomer-binding site resides in the C-terminal WH2 domain of MIM. Overexpression of mouse MIM in NIH 3T3 cells results in the disappearance of actin stress fibers and appearance of abnormal actin filament structures. These data show that MIM is an ATP-G-actin binding protein that regulates cytoskeletal dynamics in specialized mammalian cell-types.

* This study was supported by grants from the Academy of Finland, Biocentrum Helsinki, Sigrid Jusélius Foundation, and the European Molecular Biology Organization (EMBO) Young Investigator Program (to P. L.).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) AY214918.

To whom correspondence should be addressed. Tel.: 358-9-19159499; Fax: 358-9-19159366; E-mail: pekka.lappalainen@helsinki.fi.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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