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Published 28 February 2005. doi:10.1083/jcb.200409028
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 5, 789-799
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Article

 Regulation of the interaction between PIPKI{gamma} and talin by proline-directed protein kinases

Sang Yoon Lee1,2, Sergey Voronov1,2, Kresimir Letinic1,3, Angus C. Nairn4, Gilbert Di Paolo1,2, and Pietro De Camilli1,2

1 Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510
2 Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510
3 Department of Neurobiology, Yale University School of Medicine, New Haven, CT 06510
4 Department of Psychiatry, Yale University School of Medicine, New Haven, CT 06510

Correspondence to Pietro De Camilli: pietro.decamilli{at}yale.edu

The interaction of talin with phosphatidylinositol(4) phosphate 5 kinase type I{gamma} (PIPKI{gamma}) regulates PI(4,5)P2 synthesis at synapses and at focal adhesions. Here, we show that phosphorylation of serine 650 (S650) within the talin-binding sequence of human PIPKI{gamma} blocks this interaction. At synapses, S650 is phosphorylated by p35/Cdk5 and mitogen-activated protein kinase at rest, and dephosphorylated by calcineurin upon stimulation. S650 is also a substrate for cyclin B1/Cdk1 and its phosphorylation in mitosis correlates with focal adhesion disassembly. Phosphorylation by Src of the tyrosine adjacent to S650 (Y649 in human PIPKI{gamma}) was shown to enhance PIPKI{gamma} targeting to focal adhesions (Ling, K., R.L. Doughman, V.V. Iyer, A.J. Firestone, S.F. Bairstow, D.F. Mosher, M.D. Schaller, and R.A. Anderson. 2003. J. Cell Biol. 163:1339–1349). We find that Y649 phosphorylation does not stimulate directly PIPKI{gamma} binding to talin, but may do so indirectly by inhibiting S650 phosphorylation. Conversely, S650 phosphorylation inhibits Y649 phosphorylation by Src. The opposite effects of the phosphorylation of Y649 and S650 likely play a critical role in regulating synaptic function as well as the balance between cell adhesion and cell motility.

Abbreviations used in this paper: 2-D, two-dimensional; FERM, band 4.1/ezrin/radixin/moesin; ITC, isothermal titration calorimetry; PI(4,5)P2, phosphatidylinositol 4,5-bisphosphate; PIPKI{gamma}, phosphatidylinositol(4)phosphate 5-kinase type I{gamma}.


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