JBC Ideal method for primary cell transfection

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J Biol Chem, Vol. 274, Issue 51, 36288-36292, December 17, 1999

MIR Is a Novel ERM-like Protein That Interacts with Myosin Regulatory Light Chain and Inhibits Neurite Outgrowth*

Per-Anders Olsson, Laura Korhonen, Eric A. Mercer, and Dan LindholmDagger

From the Department of Neuroscience, Neurobiology, Uppsala University, Box 587 Biomedical Center, S-75123 Uppsala, Sweden

The ERM protein family members ezrin, radixin, and moesin are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. Here we report on the cloning of myosin regulatory light chain interacting protein (MIR), a protein with an ERM-homology domain and a carboxyl-terminal RING finger, that is expressed, among other tissues, in brain. MIR is distributed in cultured COS cells, in a punctated manner as shown using enhanced green fluorescent protein (EGFP)-tagged MIR and by staining with a specific antibody for MIR. In the yeast two-hybrid system and in transfected COS cells, MIR interacts with myosin regulatory light chain B, which in turn regulates the activity of the actomyosin complex. Overexpression of MIR cDNA in PC12 cells abrogated neurite outgrowth induced by nerve growth factor (NGF) without affecting TrkA signaling. The results show that MIR, a novel ERM-like protein, affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth.

* This study was supported by the Swedish Cancer Foundation (Cancerfonden) and by a EU-BIOTECH grant.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/EMBL Data Bank with accession number(s) AF187016.

Dagger To whom correspondence should be addressed. Tel.: ++46 18 4714435; Fax: ++46 18 559017; E-mail: dan.lindholm@neuro.uu.se.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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