Document Detail


Cytoskeletal protein radixin activates integrin alpha(M)beta(2) by binding to its cytoplasmic tail.
MedLine Citation:
PMID:  17321526     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Talin binding of integrins, via its band 4.1, ezrin, radixin, and moesin (FERM)-homologous domain, directly activates the integrin receptor. However, it is not known whether other FERM-containing proteins also possess such an integrin activating capability. We report here that radixin, one of the original FERM-domain proteins, binds to the membrane-proximal region of the integrin beta(2) but not alpha(M) cytoplasmic tail. Importantly, we show that radixin binding significantly enhances the adhesive activity of integrin alpha(M)beta(2). Given the distinct biological activities of radixin and talin, radixin may represent a novel talin-independent pathway for integrin activation under specific settings.
Authors:
Pingtao Tang; Chunzhang Cao; Min Xu; Li Zhang
Related Documents :
10762206 - Tissue-binding properties of a synthetic peptide dna vector targeted to cell membrane i...
19927126 - Molecular mechanism of alpha2beta1 integrin interaction with human echovirus 1.
20156196 - Transglutaminase-2: a new endostatin partner in the extracellular matrix of endothelial...
10741396 - Binding of t lymphocytes to hippocampal neurons through icam-5 (telencephalin) and char...
22766506 - Transcriptional activity of paired homeobox pax6 is enhanced by histone acetyltransfera...
2306126 - Hysteretic nature of phosphoenolpyruvate carboxylase isolated from maize.
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2007-02-15
Journal Detail:
Title:  FEBS letters     Volume:  581     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  2007 Mar 
Date Detail:
Created Date:  2007-03-16     Completed Date:  2007-05-17     Revised Date:  2007-12-03    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  1103-8     Citation Subset:  IM    
Affiliation:
Center for Vascular and Inflammatory Diseases, Department of Physiology, University of Maryland School of Medicine, 800 W Baltimore Street, Baltimore, MD 21201, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Binding Sites
CHO Cells
Cell Adhesion
Cricetinae
Cricetulus
Cytoplasm / chemistry
Cytoskeletal Proteins / metabolism*
Macrophage-1 Antigen / metabolism*
Membrane Proteins / metabolism*
Protein Binding
Transfection
Grant Support
ID/Acronym/Agency:
P01 HL54710/HL/NHLBI NIH HHS; R01 HL61589/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
0/Cytoskeletal Proteins; 0/Macrophage-1 Antigen; 0/Membrane Proteins; 144517-21-5/radixin

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


Previous Document:  Cyclic nucleotide-gated channels in plants.
Next Document:  Environmental regulation of the reproductive system in a flexibly breeding Sonoran Desert bird, the ...