PI3K‐C2α: One enzyme for two products coupling vesicle trafficking and signal transduction. Issue 14 (12th May 2015)

• Record Type: Journal Article
• Authors: Campa, Carlo C.; Franco, Irene; Hirsch, Emilio
• Is Part Of: FEBS letters. Volume 589:Issue 14(2015)
• Page Start: 1552
• Page End: 1558
• Publication Date: 2015-05-12
• Subjects: Phosphoinositide -- Class II α-isoform of phosphatidylinositol 3-kinase -- PI3K-C2α -- Endocytosis -- Exocytosis -- Signal transduction -- Vesicle trafficking; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2015.05.001
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : The spatial restriction of phosphorylated phosphoinositides generated downstream activated membrane receptors is critical for proper cell response to environmental cues. The α isoform of class II PI3Ks, PI3K‐C2α, has emerged as a modulator of receptor localization, acting both in the control of receptor endocytosis and resensitization. This unexpectedly versatile enzyme was found to differentially produce two distinct 3‐phosphorylated phosphoinositides and to selectively control distinct steps of vesicular traffic such as endocytosis and recycling. This review focuses on the latest discoveries regarding PI3K‐C2α function in vesicle trafficking and its impact on cell biology and mammalian embryonic development.