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Título

An isoform-specific PDZ-binding motif targets type I PIP5 kinase beta to the uropod and controls polarization of neutrophil-like HL60 cells

AutorMañes, Santos; Fuentes, Gloria; Peregil, Rosa M.; Rojas, A. M. ; Lacalle, Rosa Ana
Palabras claveCell migration
NHERF-1
PIPK
Polarization
Fecha de publicaciónsep-2010
EditorFederation of American Societies for Experimental Biology
CitaciónFASEB Journal 24(9): 3381-3392 (2010)
ResumenType I phosphatidylinositol 4-phosphate 5-kinase (PIP5KI)-β participates in establishing polarity during leukocyte chemotaxis. Its final 83 amino acids localize PIP5KIβ to the uropod of chemotaxing neutrophils and T cells, and interact with ezrin-radixin-moesin (ERM) proteins and EBP50 (4.1-ERM-binding phosphoprotein 50), a scaffold protein with 2 PDZ (PSD-95, disc large, ZO-1) domains. The structural motifs at the PIP5KIβ C terminus that confer signaling specificity are, nonetheless, unknown. We show that the last 4 residues of PIP5KIβ constitute an atypical PDZ-binding motif, which steers PIP5KIβ to the uropod by binding to both EBP50 PDZ domains. Molecular modeling and mutagenesis indicated that PDZ-binding motif is necessary for PIP5KIβ localization and for chemoattractant-induced neutrophil polarization. Polarity in cells that express PIP5KIβ mutants lacking the PDZ-binding motif was restored by overexpression of PIP5KIβ, but not of PIP5KIγ_i2, another isoform that localizes to the neutrophil uropod. Our results identify an isoform-specific PDZ-binding motif in PIP5KIβ, which confers specificity for PIP5KIβ signaling at the uropod during leukocyte chemotaxis.—Mañes, S., Fuentes, G., Peregil, R. M., Rojas, A. M., Lacalle, R. A. An isoform-specific PDZ-binding motif targets type I PIP5 kinase beta to the uropod and controls polarization of neutrophil-like HL60 cells.
Versión del editorhttp://doi.org/10.1096/fj.09-153106
URIhttp://hdl.handle.net/10261/153658
DOI10.1096/fj.09-153106
ISSN0892-6638
E-ISSN1530-6860
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