Calcium/calmodulin-dependent Protein Kinase II Controls Integrin alpha5beta1-mediated Cell Adhesion Through the Integrin Cytoplasmic Domain Associated protein-1alpha

Biochem Biophys Res Commun. 1998 Nov 9;252(1):46-50. doi: 10.1006/bbrc.1998.9592.


This paper provided evidence that the regulation of CHO cell adhesion on fibronectin by calcium/calmodulin-dependent protein kinase II (CaMKII) is mediated through the recently described integrin cytoplasmic domain associated protein-1alpha (ICAP-1alpha). The point mutation T38D localized within the optimal CaMKII recognition motif of ICAP-1alpha results in a strong defect in cell spreading which cannot be overcome by the inhibition of the endogenous CaMKII. This fact strongly suggests that the phosphorylation of Threonine 38 by CaMKII modulates the alpha5beta1 integrin function. Conversely, the mutation T38A produces an analog of ICAP-1alpha that cannot be phosphorylated and that stimulates cell spreading on fibronectin to a similar extent when CaMKII is inhibited.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acid Substitution
  • Animals
  • Binding Sites
  • CHO Cells
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Carrier Proteins / biosynthesis
  • Carrier Proteins / physiology*
  • Cell Adhesion*
  • Consensus Sequence
  • Cricetinae
  • Fibronectins
  • Humans
  • Intracellular Signaling Peptides and Proteins*
  • Membrane Proteins*
  • Mutagenesis, Site-Directed
  • Phosphorylation
  • Point Mutation
  • Receptors, Fibronectin / physiology*
  • Recombinant Proteins / metabolism
  • Threonine
  • Transfection


  • Carrier Proteins
  • Fibronectins
  • ITGB1BP1 protein, human
  • Intracellular Signaling Peptides and Proteins
  • Membrane Proteins
  • Receptors, Fibronectin
  • Recombinant Proteins
  • Threonine
  • Calcium-Calmodulin-Dependent Protein Kinase Type 2
  • Calcium-Calmodulin-Dependent Protein Kinases