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J Biol Chem, Vol. 274, Issue 51, 36288-36292, December 17, 1999
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.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF187016.
MIR Is a Novel ERM-like Protein That Interacts with Myosin
Regulatory Light Chain and Inhibits 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.
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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