Richard D. Smith
University of Arkansas for Medical Sciences
5 Papers
84 Citations
Richard D. Smith is an academic researcher from University of Arkansas for Medical Sciences. The author has contributed to research in topics: Golgi apparatus & Glycosylation. The author has an hindex of 5, co-authored 5 publications.
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Papers
Role of the conserved oligomeric Golgi (COG) complex in protein glycosylation
TL;DR: The Golgi apparatus is a central hub for both protein and lipid trafficking/sorting and is also a major site for glycosylation in the cell, and recent results indicate that down-regulation of COG function results in the resident Golgi Glycosyltransferases/glycosidases to be mislocalized or degraded.
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The COG complex, Rab6 and COPI define a novel Golgi retrograde trafficking pathway that is exploited by SubAB toxin.
Richard D. Smith,Rose Willett,Tetyana Kudlyk,Irina D. Pokrovskaya,Adrienne W. Paton,James C. Paton,Vladimir Lupashin +6 more
TL;DR: Surprisingly, depletion of Golgi tethers p115 and golgin‐84 that regulates two previously described coat protein I vesicle‐mediated pathways did not interfere with SubAB trafficking, indicating that SubAB is exploiting a novel COG/Rab6/COPI‐dependent retrograde trafficking pathway.
77
Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene
Brian Richardson,Richard D. Smith,Daniel Ungar,Daniel Ungar,Ayumi Nakamura,Ayumi Nakamura,Philip D. Jeffrey,Vladimir Lupashin,Frederick M. Hughson +8 more
TL;DR: Study in HeLa cells reveal that Cog4 bears a strong structural resemblance to exocyst and Dsl1p complex subunits; the emerging structural similarities provide strong evidence of a common evolutionary origin and may reflect shared mechanisms of action.
74
Mislocalization of Large ARF-GEFs as a Potential Mechanism for BFA Resistance in COG-Deficient Cells
Heather Flanagan-Steet,Steven Johnson,Richard D. Smith,Julia Bangiyeva,Vladimir Lupashin,Richard Steet +5 more
TL;DR: Biochemical analysis of GBF1 in control and BFA-treated fibroblasts demonstrated that the steady-state level and membrane recruitment is not substantially affected by COG deficiency, supporting a role for the COG complex in the localization but not membrane association ofGBF1.
9
Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery
Irina D. Pokrovskaya,Rose Willett,Richard D. Smith,Willy Morelle,Tetyana Kudlyk,Vladimir Lupashin +5 more
TL;DR: Cell surface lectin staining, examination of Golgi glycosyltransferases stability and localization, and matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) analysis were employed to investigate conserved oligomeric Golgi (COG)-dependent glycosYLation defects in HeLa cells, strongly indicating that the COG complex regulates the intra-Golgi protein movement.