Gregory Payne, Ph.D.

A Short Biography:

The Payne lab studies molecular mechanisms responsible for selective protein transport within cells, with a focus on clathrin-mediated protein traffic pathways. These conserved pathways are fundamental to normal cell function and defects in pathway components are associated with a number of diseases including cancer, heart disease, and neurodegenerative disorders. The lab has developed genetic, biochemical, structural and live cell imaging strategies to study clathrin-mediated transport in yeast, and more recently in animal cells. Projects in the lab include: 1) Endocytosis and receptor sorting. Efforts are directed at understanding the roles of specific components of the endocytic machinery. For example, the role of a membrane-bending BAR domain protein, RVS167, in endocytosis is being characterized. Novel RVS167 interaction partners have been identified, the molecular basis of interactions are being assessed by in vitro binding and structural analysis, and the role of these interactions in endocytosis are being defined in vivo, in yeast and animals cells. Another project addresses possible roles for amyloid-like interactions during endocytosis. 2) The mechanism of clathrin-coated vesicle (ccv) formation at the trans Golgi network (TGN). Clathrin adaptors play central roles in clathrin coat assembly, connecting clathrin, clathrin coat-associated proteins, and cargo. The Payne lab has defined an interaction network of TGN/endosome adaptors with hubs centered on adaptor complex-1 (AP-1) and Gga adaptor proteins, uncovered a novel process of sequential adaptor-specific ccv formation at the TGN that we term adaptor progression, and provided evidence that adaptor progression is regulated by the TGN-enriched phosphoinositide, PI4P. The molecular mechanisms responsible for phosphoinositide-mediated adaptor progression are being defined. Additional projects address the structure and function of adaptor-associated proteins in transport between the TGN and endosomes.

Work Titles
UCLA Director, Ph.D. Admissions Program, Graduate Programs in Biosciences Professor, Biological Chemistry
Education:
Degrees:
Ph.D.
Honors and Awards:
2006 Lysosomes and Endocytosis Gordon Conference, Chair
2004 Lysosomes and Endocytosis Gordon Conference, Vice-Chair
1988 Pew Scholars Award
Certifications:
Certification Type:
STEM Faculty Advisory Committee, Member
Executive Committee, Chemical Biology Interface Training Program, Member

Contact Information:

Email Address:

gpayne@mednet.ucla.edu


Lab Number:

310-825-8363

Office Phone Number:

310-206-3121

Work Address:

Laboratory
Department of Biological Chemistry
PO Box 951737
UCLa School of Medicine
Los Angeles, CA 90095

Office
Department of Biological Chemistry
PO Box 951737
UCLA School of Medicine
Los Angeles, CA 90095


Research Interest:

Vesicle-mediated protein transport within cells

The Payne lab studies molecular mechanisms responsible for selective protein transport within cells, with a focus on pathways that involve transport by clathrin-coated vesicles (ccv). These conserved pathways are fundamental to normal cell function and defects in pathway components are associated with a number of diseases including cancer, heart disease, and neurodegenerative disorders.

The lab has developed genetic, biochemical, structural and live cell imaging strategies to study clathrin-mediated transport in yeast, and more recently in animal cells.

Projects in the lab include: 1) Endocytosis and receptor sorting. Efforts are directed at understanding the roles of specific components of the endocytic machinery. For example, the role of a membrane-bending BAR domain protein, RVS167, in endocytosis is being characterized. Novel RVS167 interaction partners have been identified, the molecular basis of interactions are being assessed by in vitro binding and structural analysis, and the role of these interactions in endocytosis are being defined in vivo, in yeast and animals cells. Another project addresses possible roles for amyloid-like interactions during endocytosis. 2) The mechanism of ccv formation at the trans Golgi network (TGN). Clathrin adaptors play central roles in clathrin coat assembly, connecting clathrin, clathrin coat-associated proteins, and cargo. The Payne lab has defined an interaction network of TGN/endosome adaptors with hubs centered on adaptor complex-1 (AP-1) and Gga adaptor proteins, uncovered a novel process of sequential adaptor-specific ccv formation at the TGN that we term adaptor progression, and provided evidence that adaptor progression is regulated by the TGN-enriched phosphoinositide, PI4P. The molecular mechanisms responsible for phosphoinositide-mediated adaptor progression are being defined. Additional projects address the structure and function of adaptor-associated proteins in transport between the TGN and endosomes.

Endocytosis and protein sorting at the trans Golgi network/endosomes

The Payne lab studies molecular mechanisms responsible for selective protein transport within cells, with a focus on clathrin-mediated protein traffic pathways. These conserved pathways are fundamental to normal cell function and defects in pathway components are associated with a number of diseases including cancer, heart disease, and neurodegenerative disorders. The lab has developed genetic, biochemical, structural and live cell imaging strategies to study clathrin-mediated transport in yeast, and more recently in animal cells. Projects in the lab include: 1) Endocytosis and receptor sorting. Efforts are directed at understanding the roles of specific components of the endocytic machinery. For example, the role of a membrane-bending BAR domain protein, RVS167, in endocytosis is being characterized. Novel RVS167 interaction partners have been identified, the molecular basis of interactions are being assessed by in vitro binding and structural analysis, and the role of these interactions in endocytosis are being defined in vivo, in yeast and animals cells. Another project addresses possible roles for amyloid-like interactions during endocytosis. 2) The mechanism of clathrin-coated vesicle (ccv) formation at the trans Golgi network (TGN). Clathrin adaptors play central roles in clathrin coat assembly, connecting clathrin, clathrin coat-associated proteins, and cargo. The Payne lab has defined an interaction network of TGN/endosome adaptors with hubs centered on adaptor complex-1 (AP-1) and Gga adaptor proteins, uncovered a novel process of sequential adaptor-specific ccv formation at the TGN that we term adaptor progression, and provided evidence that adaptor progression is regulated by the TGN-enriched phosphoinositide, PI4P. The molecular mechanisms responsible for phosphoinositide-mediated adaptor progression are being defined. Additional projects address the structure and function of adaptor-associated proteins in transport between the TGN and endosomes.

Detailed Biography:

Greg Payne is a cell biologist and geneticist studying mechanisms of intracellular protein transport. He joined the Department of Biological Chemistry in the UCLA School of Medicine in 1987, received tenure in 1994, became full professor in 2000, and was departmental Vice Chair from 2004-2009. Dr. Payne received his B.S. in Cell Biology with Honors in Drama from University of Michigan in 1977 and his Ph.D. in Biochemistry in the lab of Harold Varmus from University of California, San Francisco. He was a postdoctoral with Randy Schekman at University of California, Berkeley. He has served as director of the joint Ph.D. admissions program, ACCESS, since 2008. Dr. Payne research involves cell biological, biochemical,strtuctural, molecular and standard genetic and genomic approaches to understand vesicle mediated traffic in yeast.

Publications:

Myers Margaret D, Payne Gregory S   Clathrin, adaptors and disease: insights from the yeast Saccharomyces cerevisiae Frontiers in bioscience (Landmark edition), 2013; 18: 862-91.
Hung Chao-Wei, Aoh Quyen L, Joglekar Ajit P, Payne Gregory S, Duncan Mara C   Adaptor autoregulation promotes coordinated binding within clathrin coats The Journal of biological chemistry, 2012; 287(21): 17398-407.
Daboussi Lydia, Costaguta Giancarlo, Payne Gregory S   Phosphoinositide-mediated clathrin adaptor progression at the trans-Golgi network Nature cell biology, 2012; 14(3): 239-48.
Gorynia Sabine, Lorenz Todd C, Costaguta Giancarlo, Daboussi Lydia, Cascio Duilio, Payne Gregory S   Yeast Irc6p is a novel type of conserved clathrin coat accessory factor related to small G proteins Molecular biology of the cell, 2012; 23(22): 4416-29.
van der Bliek Alexander M, Payne Gregory S   Dynamin subunit interactions revealed Developmental cell, 2010; 18(5): 687-8.
Di Pietro Santiago M, Cascio Duilio, Feliciano Daniel, Bowie James U, Payne Gregory S   Regulation of clathrin adaptor function in endocytosis: novel role for the SAM domain The EMBO journal, 2010; 29(6): 1033-44.
Anand Vikram C, Daboussi Lydia, Lorenz Todd C, Payne Gregory S   Genome-wide analysis of AP-3-dependent protein transport in yeast Molecular biology of the cell, 2009; 20(5): 1592-604.
Lorenz Todd C, Anand Vikram C, Payne Gregory S   High-throughput protein extraction and immunoblotting analysis in Saccharomyces cerevisiae Methods in molecular biology (Clifton, N.J.), 2008; 457(1): 13-27.
Duncan Mara C, Ho David G, Huang Jing, Jung Michael E, Payne Gregory S   Composite synthetic lethal identification of membrane traffic inhibitors Proc. Natl. Acad. Sci. U.S.A, 2007; 104(15): 6235-40.
Piao Hai Lan, Machado Iara M P, Payne Gregory S   NPFXD-mediated endocytosis is required for polarity and function of a yeast cell wall stress sensor Mol. Biol. Cell, 2007; 18(1): 57-65.
Mahadev Ravi K, Di Pietro Santiago M, Olson John M, Piao Hai Lan, Payne Gregory S, Overduin Michael   Structure of Sla1p homology domain 1 and interaction with the NPFxD endocytic internalization motif EMBO J, 2007; 26(7): 1963-71.
Costaguta Giancarlo, Duncan Mara C, Fernandez G Esteban, Huang Grace H, Payne Gregory S   Distinct roles for TGN/endosome epsin-like adaptors Ent3p and Ent5p Molecular biology of the cell, 2006; 17(9): 3907-20.
Parsons Ainslie B, Lopez Andres, Givoni Inmar E, Williams David E, Gray Christopher A, Porter Justin, Chua Gordon, Sopko Richelle, Brost Renee L, Ho Cheuk-Hei, Wang Jiyi, Ketela Troy, Brenner Charles, Brill Julie A, Fernandez G Esteban, Lorenz Todd C, Payne Gregory S, Ishihara Satoru, Ohya Yoshikazu, Andrews Brenda, Hughes Timothy R, Frey Brendan J, Graham Todd R, Andersen Raymond J, Boone Charles   Exploring the mode-of-action of bioactive compounds by chemical-genetic profiling in yeast Cell, 2006; 126(3): 611-25.
Fernandez G Esteban, Payne Gregory S   Laa1p, a conserved AP-1 accessory protein important for AP-1 localization in yeast Molecular biology of the cell, 2006; 17(7): 3304-17.
Zegzouti Hicham, Li Wei, Lorenz Todd C, Xie Mingtang, Payne C Thomas, Smith Kelly, Glenny Scott, Payne Gregory S, Christensen Sioux K   Structural and functional insights into the regulation of Arabidopsis AGC VIIIa kinases The Journal of biological chemistry, 2006; 281(46): 35520-30.
Duncan Mara C, Payne Gregory S   An endocytic Prk-ing brake Nature cell biology, 2005; 7(3): 210-2.
Duncan Mara C, Payne Gregory S   Cell biology: protein choreography Nature, 2005; 438(7068): 571-3.
Duncan Mara C, Payne Gregory S   ENTH/ANTH domains expand to the Golgi Trends in cell biology, 2003; 13(5): 211-5.
Duncan Mara C, Costaguta Giancarlo, Payne Gregory S   Yeast epsin-related proteins required for Golgi-endosome traffic define a gamma-adaptin ear-binding motif Nature cell biology, 2003; 5(1): 77-81.
Visapaa Ilona, Fellman Vineta, Vesa Jouni, Dasvarma Ayan, Hutton Jenna L, Kumar Vijay, Payne Gregory S, Makarow Marja, Van Coster Rudy, Taylor Robert W, Turnbull Douglass M, Suomalainen Anu, Peltonen Leena   GRACILE syndrome, a lethal metabolic disorder with iron overload, is caused by a point mutation in BCS1L American journal of human genetics, 2002; 71(4): 863-76.
Howard James P, Hutton Jenna L, Olson John M, Payne Gregory S   Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis The Journal of cell biology, 2002; 157(2): 315-26.
Dell'Angelica, EC Payne, GS   Intracellular cycling of lysosomal enzyme receptors: cytoplasmic tails' tales Cell. , 2001; 106(4): 395-8.
Bensen, ES Yeung, BG Payne, GS   Ric1p and the Ypt6p GTPase function in a common pathway required for localization of trans-Golgi network membrane proteins Molecular biology of the cell. , 2001; 12(1): 13-26.
Costaguta, G Stefan, CJ Bensen, ES Emr, SD Payne, GS   Yeast Gga coat proteins function with clathrin in Golgi to endosome transport Molecular biology of the cell. , 2001; 12(6): 1885-96.
Pishvaee, B Costaguta, G Yeung, BG Ryazantsev, 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 Nature cell biology. , 2000; 2(12): 958-63.
Bensen, E., Costaguta, G. and Payne, G.S.   Synthetic interactions with temperature-sensitive clathrin in Saccharomyces cerevisiae: roles for dynamin-related Vps1p and synaptojanin-like Inp53p in clathrin-dependent TGN membrane protein localization, Genetics, 2000; 154: 83-97.

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