Document Detail

Plexin signaling hampers integrin-based adhesion, leading to Rho-kinase independent cell rounding, and inhibiting lamellipodia extension and cell motility.
MedLine Citation:
PMID:  14734633     Owner:  NLM     Status:  MEDLINE    
Plexins encode receptors for semaphorins, molecular signals guiding cell migration, and axon pathfinding. The mechanisms mediating plexin function are poorly understood. Plexin activation in adhering cells rapidly leads to retraction of cellular processes and cell rounding "cell collapse"). Here we show that, unexpectedly, this response does not require the activity of Rho-dependent kinase (ROCK) nor the contraction of F-actin cables. Interestingly, integrin-based focal adhesive structures are disassembled within minutes upon plexin activation; this is followed by actin depolymerization and, eventually, by cellular collapse. We also show that plexin activation hinders cell attachment to adhesive substrates, blocks the extension of lamellipodia, and thereby inhibits cell migration. We conclude that plexin signaling uncouples cell substrate-adhesion from cytoskeletal dynamics required for cell migration and axon extension.
D Barberis; S Artigiani; A Casazza; S Corso; S Giordano; C A Love; E Y Jones; P M Comoglio; Luca Tamagnone
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Publication Detail:
Type:  Journal Article     Date:  2004-01-20
Journal Detail:
Title:  FASEB journal : official publication of the Federation of American Societies for Experimental Biology     Volume:  18     ISSN:  1530-6860     ISO Abbreviation:  FASEB J.     Publication Date:  2004 Mar 
Date Detail:
Created Date:  2004-03-08     Completed Date:  2004-06-01     Revised Date:  2012-02-22    
Medline Journal Info:
Nlm Unique ID:  8804484     Medline TA:  FASEB J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  592-4     Citation Subset:  IM    
Institute for Cancer Research and Treatment, University of Torino School of Medicine, Candiolo, Italy.
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MeSH Terms
Actins / metabolism
Antigens, CD*
Axons / physiology,  ultrastructure
COS Cells / physiology,  ultrastructure
Cell Movement
Cell Size
Cercopithecus aethiops
Cytoskeleton / physiology*,  ultrastructure
Focal Adhesions
Integrins / antagonists & inhibitors*
Intracellular Signaling Peptides and Proteins
Membrane Glycoproteins / physiology
Nerve Tissue Proteins*
Protein Structure, Tertiary
Protein-Serine-Threonine Kinases / physiology
Pseudopodia / physiology*
Receptors, Cell Surface / chemistry,  genetics,  physiology*
Receptors, Peptide / chemistry,  genetics,  physiology*
Recombinant Fusion Proteins / physiology
Signal Transduction / physiology*
rho-Associated Kinases
Grant Support
Reg. No./Substance:
0/Actins; 0/Antigens, CD; 0/CD100 antigen; 0/Integrins; 0/Intracellular Signaling Peptides and Proteins; 0/Membrane Glycoproteins; 0/Nerve Tissue Proteins; 0/Plxna1 protein, mouse; 0/Plxnb1 protein, mouse; 0/Receptors, Cell Surface; 0/Receptors, Peptide; 0/Recombinant Fusion Proteins; 0/Semaphorins; EC Kinases; EC Kinases

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

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