ArticleMolecular biology of the cell1995
Mapping in vivo associations of cytoplasmic proteins with integrin beta 1 cytoplasmic domain mutants.
Article in Molecular biology of the cell, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 136 citations in OpenAlex.
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- Integrin signaling in oligodendrocytes and its importance in CNS myelination.Journal of signal transduction · 2011Article
- Significance of talin in cancer progression and metastasis.International review of cell and molecular biology · 2011Review
- beta1 integrin cytoplasmic domain residues selectively modulate fibronectin matrix assembly and cell spreading through talin and Akt-1.The Journal of biological chemistry · 2009Article
- Integrin stimulation-induced hypertrophy in neonatal rat cardiomyocytes is NO-dependent.Molecular and cellular biochemistry · 2009Article
- An inhibitory role for FAK in regulating proliferation: a link between limited adhesion and RhoA-ROCK signaling.The Journal of cell biology · 2006Article
- The focal adhesion kinase (P125FAK) is constitutively active in human malignant melanoma.Oncogene · 2002Article
- Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling.The Journal of cell biology · 2002Article
- Integrins regulate the apoptotic response to DNA damage through modulation of p53.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- alpha1 Integrin cytoplasmic domain is involved in focal adhesion formation via association with intracellular proteins.The Biochemical journal · 2001Article
- Dystrophin and the cardiomyocyte membrane cytoskeleton in the healthy and failing heart.Heart failure reviews · 2000Article
- Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain.The EMBO journal · 2000Article
- The cytoplasmic tyrosines of integrin subunit beta1 are involved in focal adhesion kinase activation.Molecular and cellular biology · 2000Article
- Differential role of beta(1C) and beta(1A) integrin cytoplasmic variants in modulating focal adhesion kinase, protein kinase B/AKT, and Ras/Mitogen-activated protein kinase pathways.Molecular biology of the cell · 2000Article
- Characterization of beta2 (CD18) integrin phosphorylation in phorbol ester-activated T lymphocytes.The Biochemical journal · 1999Article
- Muscle beta1D integrin reinforces the cytoskeleton-matrix link: modulation of integrin adhesive function by alternative splicing.The Journal of cell biology · 1997Article
- Integrin alpha 6A beta 1 induces CD81-dependent cell motility without engaging the extracellular matrix migration substrate.Molecular biology of the cell · 1997Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Integrins promote formation of focal adhesions and trigger intracellular signaling pathways through cytoplasmic proteins such as talin, alpha-actinin, and focal adhesion kinase (FAK). The beta 1 integrin subunit has been shown to bind talin and alpha-actinin in in vitro assays, and these proteins may link integrin to the actin cytoskeleton either directly or through linkages to other proteins such as vinculin. However, it is unknown which of these associations are necessary in vivo for formation of focal contacts, or which regions of beta 1 integrin bind to specific cytoskeletal proteins in vivo. We have developed an in vivo assay to address these questions. Microbeads were coated with anti-chicken beta 1 antibodies to selectively cluster chicken beta 1 integrins expressed in cultured mouse fibroblasts. The ability of cytoplasmic domain mutant beta 1 integrins to induce co-localization of proteins was assessed by immunofluorescence and compared with that of wild-type integrin. As expected, mutant beta 1 lacking the entire cytoplasmic domain had a reduced ability to induce co-localization of talin, alpha-actinin, F-actin, vinculin, and FAK. The ability of beta 1 integrin to co-localize talin and FAK was found to require a sequence near the C-terminus of beta 1. The region of beta 1 required to co-localize alpha-actinin was found to reside in a different sequence, several amino acids further from the C-terminus of beta 1. Deletion of 13 residues from the C-terminus blocked co-localization of talin, FAK, and actin, but not alpha-actinin. Association of alpha-actinin with clustered integrin is therefore not sufficient to induce the co-localization of F-actin.
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