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Functional activities and cellular localization of the ezrin, radixin, moesin (ERM) and RING zinc finger domains in MIR
Author(s) -
Bornhauser Beat C,
Johansson Cecilia,
Lindholm Dan
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01010-x
Subject(s) - moesin , radixin , microbiology and biotechnology , ezrin , neurite , cytoskeleton , chemistry , myosin , ring (chemistry) , cell , biology , biochemistry , in vitro , organic chemistry
Myosin regulatory light chain interacting protein (MIR) belongs to the ezrin, radixin, moesin (ERM) family of proteins involved in membrane cytoskeleton interactions and cell dynamics. MIR contains, beside the ERM domain, a RING zinc finger region. Immunocytochemistry showed that full‐length MIR and the subdomains localize differently in cells. Cell fractionation revealed a similar distribution of full‐length MIR and the RING domain protein in the Triton X‐100‐insoluble fraction. The neurite outgrowth inhibitory activity of MIR was attributed to the RING domain. MIR levels were controlled in the cells depending on the intact RING domain and proteasome activity. The dynamic regulation of MIR contributes to its effects on neurite outgrowth and cell motility.