Vladimir V. Lupashin
Associate Professor
Ph.D., Russian Academy of Sciences
Office: (501) 603-1170
Lab: (501) 603-1171
Email: vvlupashin@uams.edu

Our laboratory is interested in understanding the molecular mechanisms responsible for the generation and maintenance of intra-cellular membrane-bounded compartments. Specifically, we study the mechanisms and machinery that maintain the high degree of specificity inherent in transport vesicle docking in the secretory pathway. We are also interested in the mechanism of retention and retrieval of integral membrane proteins in different sub-compartments of the Golgi apparatus.

Golgi vesicle tethering factors were the major focus of our recent research. We have discovered and characterize the evolutionarily Conserved Oligomeric Golgi (COG) complex that plays a major role on the intra-Golgi retrograde membrane trafficking. We have shown that the COG complex interacts with SNAREs, Rab-GTP and the COPI vesicle coat. Cog3p knock-down in Hela cells is accompanied by accumulation of COG complex dependent (CCD) vesicles carrying v-SNAREs, cis-Golgi glycoprotein GPP130 and cis/medial Golgi glycosylation enzymes. A prolonged block in CCD vesicles tethering is accompanied by extensive fragmentation of the Golgi ribbon. Fragmented Golgi membranes maintained their juxtanuclear localization, cisternal organization and are competent for the anterograde trafficking of VSVG protein to the plasma membrane. In a contrast, Cog3p knock-down resulted in inhibition of retrograde trafficking of the Shiga toxin. We are currently characterizing the complex further through biochemical, molecular genetic and cell biological methods.
By using a number of different approaches in both mammalian and yeast systems we hope to shed new light into the vesicular transport mechanism of eukaryotic cells.

Dr. Lupashin's Laboratory Homepage

Representative Publications

Smith RD, Willett R, Kudlyk T, Pokrovskaya I, Paton AW, Paton JC, Lupashin VV. The COG complex, Rab6 and COPI define a novel Golgi retrograde trafficking pathway that is exploited by SubAB toxin. Traffic 2009 Oct;10(10):1502-17

Richardson BC, Smith RD, Ungar D, Nakamura A, Jeffrey PD, Lupashin VV, Hughson FM. Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene. Proc Natl Acad Sci U S A 2009 Aug 11;106(32):13329-34.
 
Ahmed BA, Bukhari IA, Jeffus BC, Harney JT, Thyparambil S, Ziu E, Fraer M, Rusch NJ, Zimniak P, Lupashin V, Tang D, Kilic F. The cellular distribution of serotonin transporter is impeded on serotonin-altered vimentin network. PLoS One 2009;4(3):e4730. Epub 2009 Mar 9.

Smith RD, Lupashin VV: Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation. Carbohydr Res 2008, 343(12):2024-2031.

Sun Y, Shestakova A, Hunt L, Sehgal S, Lupashin V, Storrie B: Rab6 regulates both ZW10/RINT-1 and conserved oligomeric Golgi complex-dependent Golgi trafficking and homeostasis. Mol Biol Cell 2007, 18(10):4129-4142.

Shestakova A, Suvorova E, Pavliv O, Khaidakova G, Lupashin V: Interaction of the conserved oligomeric Golgi complex with t-SNARE Syntaxin5a/Sed5 enhances intra-Golgi SNARE complex stability. J Cell Biol 2007, 179(6):1179-1192.

Link to Dr. Lupashin at PubMed

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