Title
The alpha 6A beta 1 and alpha 6B beta 1 integrin variants signal differences in the tyrosine phosphorylation of paxillin and other proteins
UMMS Affiliation
Department of Cancer Biology
Publication Date
1995-10-06
Document Type
Article
Subjects
Animals; Cell Adhesion Molecules; Cell Line; Cytoplasm; Cytoskeletal Proteins; *Genetic Variation; Humans; Integrin alpha6beta1; Integrins; Laminin; Mice; Paxillin; Phosphoproteins; Phosphorylation; Proteins; Signal Transduction; Transfection; Tyrosine
Disciplines
Amino Acids, Peptides, and Proteins | Cancer Biology | Neoplasms
Abstract
Integrin receptors can mediate transmembrane signaling in response to ligand binding. To further examine the role of the integrin alpha subunit in these signaling functions, we assessed the contribution of the alpha 6 cytoplasmic domain variants to the signaling properties of the alpha 6 beta 1 integrin using P388D1 cells that had been transfected with either the alpha 6A or the alpha 6B cDNA. The alpha 6A beta 1 and alpha 6B beta 1 receptors induced marked quantitative differences in the tyrosine phosphorylation of several proteins after binding to laminin. Specifically, the alpha 6A cytoplasmic domain was more effective than the alpha 6B cytoplasmic domain in inducing the tyrosine phosphorylation of three major proteins (molecular mass, 120, 110, and 76 kDa). In addition to these proteins, we also observed that the tyrosine phosphorylation of the cytoskeletal protein paxillin was increased significantly more by alpha 6A beta 1 integrin-mediated adhesion to laminin than by that of alpha 6B beta 1. This differential pattern of tyrosine phosphorylation induction does not appear to be a secondary event initiated by cell shape changes. Also, differences in tyrosine phosphorylation in the alpha 6 transfectants were not evident in response to attachment to other substrates. These findings provide biochemical evidence for functional differences between alpha subunit cytoplasmic domain variants of the same integrin.
DOI of Published Version
10.1074/jbc.270.40.23648
Source
J Biol Chem. 1995 Oct 6;270(40):23648-52.
Journal/Book/Conference Title
The Journal of biological chemistry
Related Resources
PubMed ID
7559532
Repository Citation
Shaw LM, Turner CE, Mercurio AM. (1995). The alpha 6A beta 1 and alpha 6B beta 1 integrin variants signal differences in the tyrosine phosphorylation of paxillin and other proteins. Cancer Biology Publications and Presentations. https://doi.org/10.1074/jbc.270.40.23648. Retrieved from https://escholarship.umassmed.edu/cancerbiology_pp/138