TY - JOUR
T1 - Integrins interact with focal adhesions through multiple distinct pathways
AU - David, Frank S.
AU - Zage, Peter E.
AU - Marcantonio, Eugene E.
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1999
Y1 - 1999
N2 - Integrin signaling involves oligomerization and a transmembrane conformational change induced by receptor occupancy. Previous work has shown that subsets of focal adhesion-associated proteins are recruited to integrins as a result of clustering, ligand binding, or both. However, it is unclear whether these discrete subsets reflect the differential binding of cytoplasmic proteins to the integrin or whether a single protein or set of proteins binds the integrin and is differentially activated by receptor occupancy or clustering. To address this question, we made mutations of the β1 integrin cytoplasmic domain in the context of a single subunit chimera and studied their activation of various known integrin-mediated signaling pathways. We show here that the indirect association of the integrin with actin is distinct from its interactions with both preformed focal adhesions and FAK. Therefore, multiple independent signaling pathways exist from the integrin to the focal adhesion, which may reflect the association of independent factors with the integrin β1 cytoplasmic domain.
AB - Integrin signaling involves oligomerization and a transmembrane conformational change induced by receptor occupancy. Previous work has shown that subsets of focal adhesion-associated proteins are recruited to integrins as a result of clustering, ligand binding, or both. However, it is unclear whether these discrete subsets reflect the differential binding of cytoplasmic proteins to the integrin or whether a single protein or set of proteins binds the integrin and is differentially activated by receptor occupancy or clustering. To address this question, we made mutations of the β1 integrin cytoplasmic domain in the context of a single subunit chimera and studied their activation of various known integrin-mediated signaling pathways. We show here that the indirect association of the integrin with actin is distinct from its interactions with both preformed focal adhesions and FAK. Therefore, multiple independent signaling pathways exist from the integrin to the focal adhesion, which may reflect the association of independent factors with the integrin β1 cytoplasmic domain.
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U2 - 10.1002/(SICI)1097-4652(199910)181:1<74::AID-JCP8>3.0.CO;2-H
DO - 10.1002/(SICI)1097-4652(199910)181:1<74::AID-JCP8>3.0.CO;2-H
M3 - Article
C2 - 10457355
AN - SCOPUS:0032774768
VL - 181
SP - 74
EP - 82
JO - Journal of Cellular Physiology
JF - Journal of Cellular Physiology
SN - 0021-9541
IS - 1
ER -