Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin - PubMed (original) (raw)
. 2002 Nov 7;420(6911):85-9.
doi: 10.1038/nature01147.
Affiliations
- PMID: 12422219
- DOI: 10.1038/nature01147
Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin
Gilbert Di Paolo et al. Nature. 2002.
Abstract
Membrane phosphoinositides control a variety of cellular processes through the recruitment and/or regulation of cytosolic proteins. One mechanism ensuring spatial specificity in phosphoinositide signalling is the targeting of enzymes that mediate their metabolism to specific subcellular sites. Phosphatidylinositol phosphate kinase type 1 gamma (PtdInsPKI gamma) is a phosphatidylinositol-4-phosphate 5-kinase that is expressed at high levels in brain, and is concentrated at synapses. Here we show that the predominant brain splice variant of PtdInsPKI gamma (PtdInsPKI gamma-90) binds, by means of a short carboxy-terminal peptide, to the FERM domain of talin, and is strongly activated by this interaction. Talin, a principal component of focal adhesion plaques, is also present at synapses. PtdInsPKI gamma-90 is expressed in non-neuronal cells, albeit at much lower levels than in neurons, and is concentrated at focal adhesion plaques, where phosphatidylinositol-4,5-bisphosphate has an important regulatory role. Overexpression of PtdInsPKI gamma-90, or expression of its C-terminal domain, disrupts focal adhesion plaques, probably by local disruption of normal phosphoinositide balance. These findings define an interaction that has a regulatory role in cell adhesion and suggest new similarities between molecular interactions underlying synaptic junctions and general mechanisms of cell adhesion.
Comment in
- Cell adhesion: a FERM grasp of membrane dynamics.
Liddington RC, Bankston LA, de Pereda JM. Liddington RC, et al. Curr Biol. 2003 Feb 4;13(3):R94-5. doi: 10.1016/s0960-9822(03)00035-6. Curr Biol. 2003. PMID: 12573235
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