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DESCRIPTION:Department of Anatomy and Cell Biology\n	& Department of Pharmac
 ology and Therapeutics\n\nHosted by Dr. John Presley\, Anatomy & Cell Biol
 ogy\n	& Dr. Claudio Cuello\, Pharmacology\n\nOn the move: mechanisms and fu
 nctions\n	of lysosome positioning\n\nDr. Juan Bonifacino\n	National Institut
 e of Health (NIH)\, USA\n	Distinguished Investigator & Associate Scientific
  Director\,\n	Cell Biology & Neurobiology Branch\n\nWednesday\, April 19\, 
 2017\n	11:30 am\n	Strathcona Anatomy Building\, 3640 University Street\n	Char
 les Leblond Amphitheatre (Room M-1)\n\n\n	www.mcgill.ca/anatomy/seminars\n	a
 natomysec.med [at] mcgill.ca\n\nResearch Summary:\n\nLysosomes are membran
 e-bound organelles whose main function is the degradation of biomacromolec
 ules delivered by way of endocytosis\, biosynthetic transport and autophag
 y. In addition\, lysosomes participate in many other cellular processes\, 
 including lipid homeostasis\, cell adhesion and migration\, plasma membran
 e repair\, detoxification\, apoptosis\, metabolic signaling and gene regul
 ation. In my presentation\, I will describe recent work from my laboratory
  on a novel aspect of lysosome biology: their positioning and motility wit
 hin the cytoplasm. Indeed\, lysosomes move back and forth between the cent
 er and the periphery of the cells. Outward movement is driven by kinesins\
 , whereas inward movement is driven by dynein. The mechanisms by which lys
 osomes are coupled to these microtubule motors are incompletely understood
 . We obtained unexpected insights into the coupling of lysosomes to kinesi
 ns in the course of our studies on the BLOC-1 complex that is defective in
  some types of the hypopigmentation and bleeding disorder Hermansky-Pudlak
  syndrome (HPS). Affinity purification and mass spectrometry analyses usin
 g the BLOS2 subunit of BLOC-1 as bait led us to discover a related eight-s
 ubunit complex named BORC (for BLOC-one-related complex). We found that BO
 RC associates with the lysosomal membrane\, where it functions to recruit 
 the small GTPase Arl8. This initiates a chain of interactions that promote
 s kinesin-dependent movement of lysosomes toward the plus ends of microtub
 ules in the cell periphery. Further studies showed that BORC-dependent dis
 persal of lysosomes is required for autophagy\, cholesterol transport\, ce
 ll adhesion and migration\, and nutrient signaling. These experiments thus
  uncovered a molecular machinery involved in moving lysosomes to the cell 
 periphery\, and highlighted the importance of this machinery in the regula
 tion of many critical cellular processes.\n
DTSTART:20170419T153000Z
DTEND:20170419T163000Z
SUMMARY:Dr. Juan Bonifacino\, NIH\, Cell Biology & Neurobiology
URL:/pharma/channels/event/dr-juan-bonifacino-nih-cell
 -biology-neurobiology-267528
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