Document Detail

MAGI-1 is required for Rap1 activation upon cell-cell contact and for enhancement of vascular endothelial cadherin-mediated cell adhesion.
MedLine Citation:
PMID:  16339077     Owner:  NLM     Status:  MEDLINE    
Rap1 is a small GTPase that regulates adherens junction maturation. It remains elusive how Rap1 is activated upon cell-cell contact. We demonstrate for the first time that Rap1 is activated upon homophilic engagement of vascular endothelial cadherin (VE-cadherin) at the cell-cell contacts in living cells and that MAGI-1 is required for VE-cadherin-dependent Rap1 activation. We found that MAGI-1 localized to cell-cell contacts presumably by associating with beta-catenin and that MAGI-1 bound to a guanine nucleotide exchange factor for Rap1, PDZ-GEF1. Depletion of MAGI-1 suppressed the cell-cell contact-induced Rap1 activation and the VE-cadherin-mediated cell-cell adhesion after Ca2+ switch. In addition, relocation of vinculin from cell-extracellular matrix contacts to cell-cell contacts after the Ca2+ switch was inhibited in MAGI-1-depleted cells. Furthermore, inactivation of Rap1 by overexpression of Rap1GAPII impaired the VE-cadherin-dependent cell adhesion. Collectively, MAGI-1 is important for VE-cadherin-dependent Rap1 activation upon cell-cell contact. In addition, once activated, Rap1 upon cell-cell contacts positively regulate the adherens junction formation by relocating vinculin that supports VE-cadherin-based cell adhesion.
Atsuko Sakurai; Shigetomo Fukuhara; Akiko Yamagishi; Keisuke Sako; Yuji Kamioka; Michitaka Masuda; Yoshikazu Nakaoka; Naoki Mochizuki
Related Documents :
16686687 - Cell-to-cell electrical interactions during early and late repolarization.
20512937 - Enhanced connexin 43 expression delays intra-mitotic duration and cell cycle traverse i...
20188437 - The protoplasmic or exoplasmic face association of tight junction particles cannot pred...
19357237 - Modulation of cx46 hemichannels by nitric oxide.
211417 - Transmission of hormonal stimulation by cell-to-cell communication.
19567817 - Proteomic identification of aldo-keto reductase akr1b10 induction after treatment of co...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-12-07
Journal Detail:
Title:  Molecular biology of the cell     Volume:  17     ISSN:  1059-1524     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2006-01-25     Completed Date:  2006-04-07     Revised Date:  2013-06-07    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  966-76     Citation Subset:  IM    
Department of Structural Analysis, National Cardiovascular Center Research Institute, Suita, Osaka 565-8565, Japan.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Adaptor Proteins, Signal Transducing / chemistry,  metabolism,  physiology*
Cadherins / metabolism*
Cell Adhesion
Cell Adhesion Molecules, Neuronal
Cell Line
Endothelium, Vascular / cytology,  metabolism*
Enzyme Activation
Guanine Nucleotide Exchange Factors / metabolism
Membrane Proteins / chemistry,  metabolism,  physiology*
Models, Biological
Nerve Tissue Proteins / metabolism
Protein Structure, Tertiary
Sequence Deletion
rap1 GTP-Binding Proteins / metabolism*
Reg. No./Substance:
0/Adaptor Proteins, Signal Transducing; 0/Cadherins; 0/Cell Adhesion Molecules, Neuronal; 0/Guanine Nucleotide Exchange Factors; 0/MAGI1 protein, human; 0/Membrane Proteins; 0/Nerve Tissue Proteins; 0/RAPGEF2 protein, human; EC GTP-Binding Proteins

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

Previous Document:  Contractile ring-independent localization of DdINCENP, a protein important for spindle stability and...
Next Document:  Hsp27 enhances recovery of splicing as well as rephosphorylation of SRp38 after heat shock.