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SUMMARY:The phospholipid PI(3\,4)P2 is an apical identity determinant - Dr
  David Bryant\; Head of Epithelial Polarity Lab\, Institute of Cancer Scie
 nces / CRUK Beatson Institute\, Glasgow 
DTSTART:20190326T120000Z
DTEND:20190326T130000Z
UID:TALK113053@talks.cam.ac.uk
CONTACT:Bobbie Claxton
DESCRIPTION:Apical-basal polarization is essential for epithelial tissue f
 ormation\, segregating cortical domains to perform distinct physiological 
 functions. Cortical lipid asymmetry has emerged as a determinant of cell p
 olarization. We report a network of phosphatidylinositol phosphate (PIP)-m
 odifying enzymes\, some of which are transcriptionally induced upon embedd
 ing epithelial cells in extracellular matrix\, and that are essential for 
 apical-basal polarization. Unexpectedly\, we find that PI(3\,4)P2 localiza
 tion and function is distinct from the basolateral determinant PI(3\,4\,5)
 P3. PI(3\,4)P2 localizes to the apical surface\, and Rab11a-positive apica
 l recycling endosomes. PI(3\,4)P2 is produced by the 5-phosphatase SHIP1 a
 nd Class-II PI3-Kinases to recruit the endocytic regulatory protein SNX9 t
 o basolateral domains that are being remodeled into apical surfaces. Pertu
 rbing PI(3\,4)P2 levels results in defective polarization through subcorti
 cal retention of apically destined vesicles at apical membrane initiation 
 sites. We conclude that PI(3\,4)P2 is a determinant of apical membrane ide
 ntity.
LOCATION:Babraham - The Cambridge Building\; Queen Edith Room
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