Integrins interact with focal adhesions through multiple distinct pathways

Frank S. David, Peter E. Zage, Eugene E. Marcantonio

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)74-82
Number of pages9
JournalJournal of Cellular Physiology
Volume181
Issue number1
DOIs
StatePublished - 1999

ASJC Scopus subject areas

  • Physiology
  • Clinical Biochemistry
  • Cell Biology

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