Document Detail


Functional activities and cellular localization of the ezrin, radixin, moesin (ERM) and RING zinc finger domains in MIR.
MedLine Citation:
PMID:  14550572     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Beat C Bornhauser; Cecilia Johansson; Dan Lindholm
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  553     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2003 Oct 
Date Detail:
Created Date:  2003-10-10     Completed Date:  2003-11-12     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  195-9     Citation Subset:  IM    
Affiliation:
Department of Neuroscience, Neurobiology, Uppsala University, Biomedical Centre, Sweden.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Blood Proteins / chemistry*
COS Cells
Carrier Proteins / chemistry*,  metabolism*
Cytoskeletal Proteins / chemistry*
Humans
Membrane Proteins / chemistry*
Microfilament Proteins / chemistry*
Neurites / metabolism
Phosphoproteins / chemistry*
Protein Structure, Tertiary
Protein Transport
Structure-Activity Relationship
Tumor Cells, Cultured
Ubiquitin / metabolism
Ubiquitin-Protein Ligases
Zinc Fingers*
Chemical
Reg. No./Substance:
0/Blood Proteins; 0/Carrier Proteins; 0/Cytoskeletal Proteins; 0/Membrane Proteins; 0/Microfilament Proteins; 0/Phosphoproteins; 0/Ubiquitin; 0/ezrin; 144131-77-1/moesin; 144517-21-5/radixin; EC 6.3.2.-/MYLIP protein, human; EC 6.3.2.19/Ubiquitin-Protein Ligases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Ubiquitin activated tumor necrosis factor receptor associated factor-6 (TRAF6) is recycled via deubi...
Next Document:  Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subuni...