Regulation of extranuclear PtdIns5 P  production by phosphatidylinositol phosphate 4‐kinase 2α | Zendy

Wilcox Andrew | Zendy; Hinchliffe Katherine A. | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research