Regulation of the interaction between PIPKI gamma and talin by proline-directed protein kinases.
Regulation of the interaction between PIPKI gamma and talin by proline-directed protein kinases.
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DOI:
10.1083/jcb.200409028
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发表时间:
2005-02-28
期刊:
影响因子:
--
通讯作者:
De Camilli P
中科院分区:
文献类型:
--
作者:
Lee SY;Voronov S;Letinic K;Nairn AC;Di Paolo G;De Camilli P
The interaction of talin with phosphatidylinositol(4) phosphate 5 kinase type Iγ (PIPKIγ) 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 PIPKIγ 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 PIPKIγ) was shown to enhance PIPKIγ 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 PIPKIγ 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.
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影响因子:
4.8
作者:
Bauerfeind, R;Takei, K;De Camilli, P
通讯作者:
De Camilli, P
影响因子:
4.8
作者:
Hsieh-Wilson, LC;Benfenati, F;Greengard, P
通讯作者:
Greengard, P
影响因子:
64.8
作者:
Di Paolo, G;Pellegrini, L;De Camilli, P
通讯作者:
De Camilli, P
DOI:
10.1083/jcb.200301006
发表时间:
2003-07-07
期刊:
The Journal of cell biology
影响因子:
--
作者:
Krauss M;Kinuta M;Wenk MR;De Camilli P;Takei K;Haucke V
通讯作者:
Haucke V
影响因子:
4.8
作者:
Floyd, SR;Porro, EB;De Camilli, P
通讯作者:
De Camilli, P