Association of beta 1 integrin with protein kinase activity in large detergent resistant complexes.
Integrins play a critical role in cell adhesion and mediate cell signaling. This report identifies the association of serine protein kinase activity with the beta 1 integrin by immunoprecipitation and phosphoamino acid analysis techniques. Reprecipitation techniques suggested that the serine kinase activity was not a member of the protein kinase C family. By gel filtration, most of the protein kinase activity associated with beta 1 integrin as well as most of the cell-surface beta 1 integrin was present in large detergent resistant complexes. These results suggest that serine protein kinase activity associated with the beta 1 integrin may play a role in signaling via the beta 1 integrin.
Skubitz
A P
AP
Department of Laboratory Medicine and Pathology and the Biomedical Engineering Center, University of Minnesota Medical School, Minneapolis 55455, USA. skubi002@tc.umn.edu
Campbell
K D
KD
Goueli
S
S
Skubitz
K M
KM
D002850:Chromatography, Gel; D003902:Detergents; D004789:Enzyme Activation; D006801:Humans; D019012:Integrin beta1 / Q000096:biosynthesis / Q000378:metabolism*; D046911:Macromolecular Substances; D008565:Membrane Proteins / Q000096:biosynthesis; D019606:Phosphoamino Acids / Q000032:analysis; D011493:Protein Kinase C / Q000032:analysis; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D014407:Tumor Cells, Cultured
D003902:Detergents; D019012:Integrin beta1; D046911:Macromolecular Substances; D008565:Membrane Proteins; D019606:Phosphoamino Acids; D017346:Protein Serine-Threonine Kinases; D011493:Protein Kinase C