Research in Dr. Gregory Payne's lab addresses mechanisms of clathrin-mediated protein traffic, with an emphasis on endocytosis and transport between the trans Golgi network and endosomes. Transport through these pathways is important for down-regulation of growth-signaling receptors and for maturation of growth factors and other molecules important for cell-cell communication. Because the process and molecular machinery of clathrin-mediated transport is conserved in eukaryotic cells, the Payne lab uses the budding yeast Saccaromyces cerevisiae as a model organism.
The Payne lab applies molecular genetics, systematic genome-wide genetic approaches, proteomics, chemical genetics and time-lapse live cell imaging to understand how clathrin coated vesicles are formed and how proteins are selected for transport in these vesicles.
Selected Cancer-Related Publications:
Mahadev RK, Di Pietro SM, Olson JM, Piao HL, Payne GS, Overduin M. Solution structure of Sla1 Homology domain 1 and interaction with the NPFxD endocytic internalization motif. EMBO J. 2007 Apr 4;26(7):1963-71. Epub 2007 Mar 15.
Duncan MC, Ho DG, Huang J, Jung ME, Payne GS. Composite synthetic lethal identification of membrane traffic inhibitors. Proc Natl Acad Sci U S A. 2007 Apr 10;104(15):6235-40. Epub 2007 Apr 2.
Duncan MC, Costaguta G, Payne GS. Yeast epsin-related proteins required for Golgi-endosome traffic define a gamma-adaptin ear-binding motif. Nat Cell Biol. 2003 Jan;5(1):77-81.
Howard JP, Hutton JL, Olson JM, Payne GS. Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis. J Cell Biol. 2002 Apr 15;157(2):315-26. Epub 2002 Apr 8.
Pishvaee B, Costaguta G, Yeung BG, Ryanzatsev S, Greener T., Greene LE, Eisenberg E., McCaffery JM, Payne GS. A yeast DNA J protein required for uncoating of clathrin-coated vesicles in vivo. Nat Cell Biol. 2000 Dec;2(12):958-63.