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Regulation of extranuclear PtdIns5 P production by phosphatidylinositol phosphate 4‐kinase 2α
Author(s) -
Wilcox Andrew,
Hinchliffe Katherine A.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.03.022
Subject(s) - phosphatidylinositol , inositol , microbiology and biotechnology , phosphorylation , kinase , inositol phosphate , chemistry , stimulation , biochemistry , biology , endocrinology , receptor
Cellular levels of the phosphoinositide PtdIns5 P are regulated by agonist stimulation, but the mechanisms controlling turnover of this lipid, and the subcellular location of the regulated PtdIns5 P pool(s), remain poorly understood. Here we show that enhanced tyrosine phosphorylation robustly increases cellular PtdIns5 P levels. Moreover, unlike PtdIns5 P production enhanced by cell stress, we show that this pool of PtdIns5 P is specifically regulated by the inositol lipid kinase PIP4K2a.