Purified integrin adhesion complexes exhibit actin-polymerization activity.
Curr Biol
; 16(3): 242-51, 2006 Feb 07.
Article
in En
| MEDLINE
| ID: mdl-16461277
ABSTRACT
BACKGROUND:
Cell adhesion and motility are accomplished through a functional linkage of the extracellular matrix with the actin cytoskeleton via adhesion complexes composed of integrin receptors and associated proteins. To determine whether this linkage is attained actively or passively, we isolated integrin complexes from nonadherent hematopoietic cells and determined their influence on the polymerization of actin.RESULTS:
We observed that alpha(V)beta3 complexes are capable of dramatically accelerating the rate of actin assembly, resulting in actin fibers tethered at their growing ends by clustered integrins. The ability to enhance actin polymerization was dependent upon Arg-Gly-Asp-ligand-induced beta3 tyrosine phosphorylation, agonist-induced cellular activation, sequestration of Diaphanous formins, and clustering of the receptor.CONCLUSIONS:
These results suggest that adhesion complexes actively promote actin assembly from their cytosolic face in order to establish a mechanical linkage with the extracellular matrix.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Signal Transduction
/
Cell Adhesion Molecules
/
Integrins
/
Cell Adhesion
/
Cell Movement
/
Actins
/
Extracellular Matrix
Limits:
Animals
/
Humans
Language:
En
Journal:
Curr Biol
Journal subject:
BIOLOGIA
Year:
2006
Document type:
Article
Affiliation country:
United States