Emilio Hirsch, Ph.D. - "PI3KC2A: lipid kinase and spindle scaffold in ciliopathies and cancer"
Dec 20, 2016
from 02:30 PM to 03:30 PM
|Where||Tigem Auditorium Vesuvius|
|Contact Name||Brunella Franco|
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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. On the other hand, this protein is a scaffold protein involved in the organization of the mitotic spindle as well as in cancer development and sensitivity to anticancer agents targeting microtubule. This double role shows how evolution can merge different activities and allow protein moonlighting in unrelated cellular functions.