Faculty Opinions recommendation of The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy.

2010 ◽  
Author(s):  
Judith Klumperman ◽  
Fulvio Reggiori
Keyword(s):  
Golgi Complex ◽  
Membrane Vesicle ◽  
Vesicle Formation ◽  
Double Membrane ◽  
Conserved Oligomeric Golgi Complex ◽  
Conserved Oligomeric Golgi

scholarly journals The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy

2010 ◽  
Vol 188 (1) ◽  
pp. 101-114 ◽  
Author(s):  
Wei-Lien Yen ◽  
Takahiro Shintani ◽  
Usha Nair ◽  
Yang Cao ◽  
Brian C. Richardson ◽  
...  
Keyword(s):  
Membrane Vesicle ◽  
Autophagosome Formation ◽  
Double Membrane ◽  
Complex Part ◽  
Cog Complex ◽  
Conserved Oligomeric Golgi Complex ◽  
Conserved Oligomeric Golgi ◽  
Critical Components ◽  
Molecular Components ◽  
Related Proteins

Macroautophagy is a catabolic pathway used for the turnover of long-lived proteins and organelles in eukaryotic cells. The morphological hallmark of this process is the formation of double-membrane autophagosomes that sequester cytoplasm. Autophagosome formation is the most complex part of macroautophagy, and it is a dynamic event that likely involves vesicle fusion to expand the initial sequestering membrane, the phagophore; however, essentially nothing is known about this process including the molecular components involved in vesicle tethering and fusion. In this study, we provide evidence that the subunits of the conserved oligomeric Golgi (COG) complex are required for double-membrane cytoplasm to vacuole targeting vesicle and autophagosome formation. COG subunits localized to the phagophore assembly site and interacted with Atg (autophagy related) proteins. In addition, mutations in the COG genes resulted in the mislocalization of Atg8 and Atg9, which are critical components involved in autophagosome formation.

scholarly journals The ER v-SNAREs are required for GPI-anchored protein sorting from other secretory proteins upon exit from the ER

2003 ◽  
Vol 162 (3) ◽  
pp. 403-412 ◽  
Author(s):  
Pierre Morsomme ◽  
Cristina Prescianotto-Baschong ◽  
Howard Riezman
Keyword(s):  
Golgi Complex ◽  
Protein Sorting ◽  
Secretory Proteins ◽  
Rab Gtpase ◽  
Cargo Protein ◽  
Conserved Oligomeric Golgi Complex ◽  
Sorting Process ◽  
Conserved Oligomeric Golgi

Glycosylphosphatidylinositol (GPI)-anchored proteins exit the ER in distinct vesicles from other secretory proteins, and this sorting event requires the Rab GTPase Ypt1p, tethering factors Uso1p, and the conserved oligomeric Golgi complex. Here we show that proper sorting depended on the vSNAREs, Bos1p, Bet1p, and Sec22p. However, the t-SNARE Sed5p was not required for protein sorting upon ER exit. Moreover, the sorting defect observed in vitro with bos1–1 extracts was also observed in vivo and was visualized by EM. Finally, transport and maturation of the GPI-anchored protein Gas1p was specifically affected in a bos1–1 mutant at semirestrictive temperature. Therefore, we propose that v-SNAREs are part of the cargo protein sorting machinery upon exit from the ER and that a correct sorting process is necessary for proper maturation of GPI-anchored proteins.

scholarly journals Conserved oligomeric Golgi complex specifically regulates the maintenance of Golgi glycosylation machinery

Glycobiology ◽  
2011 ◽  
Vol 21 (12) ◽  
pp. 1554-1569 ◽  
Author(s):  
Irina D Pokrovskaya ◽  
Rose Willett ◽  
Richard D Smith ◽  
Willy Morelle ◽  
Tetyana Kudlyk ◽  
...  
Keyword(s):  
Golgi Complex ◽  
Conserved Oligomeric Golgi Complex ◽  
Conserved Oligomeric Golgi

scholarly journals Atg27 Is Required for Autophagy-dependent Cycling of Atg9

2007 ◽  
Vol 18 (2) ◽  
pp. 581-593 ◽  
Author(s):  
Wei-Lien Yen ◽  
Julie E. Legakis ◽  
Usha Nair ◽  
Daniel J. Klionsky
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Golgi Complex ◽  
Transmembrane Protein ◽  
Eukaryotic Cells ◽  
Vesicle Formation ◽  
Catabolic Pathway ◽  
Autophagosome Formation ◽  
Yeast Saccharomyces Cerevisiae ◽  
Double Membrane ◽  
Selective Autophagy

Autophagy is a catabolic pathway for the degradation of cytosolic proteins or organelles and is conserved among all eukaryotic cells. The hallmark of autophagy is the formation of double-membrane cytosolic vesicles, termed autophagosomes, which sequester cytoplasm; however, the mechanism of vesicle formation and the membrane source remain unclear. In the yeast Saccharomyces cerevisiae, selective autophagy mediates the delivery of specific cargos to the vacuole, the analog of the mammalian lysosome. The transmembrane protein Atg9 cycles between the mitochondria and the pre-autophagosomal structure, which is the site of autophagosome biogenesis. Atg9 is thought to mediate the delivery of membrane to the forming autophagosome. Here, we characterize a second transmembrane protein Atg27 that is required for specific autophagy in yeast. Atg27 is required for Atg9 cycling and shuttles between the pre-autophagosomal structure, mitochondria, and the Golgi complex. These data support a hypothesis that multiple membrane sources supply the lipids needed for autophagosome formation.

scholarly journals Early Stages of the Secretory Pathway, but Not Endosomes, Are Required for Cvt Vesicle and Autophagosome Assembly in Saccharomyces cerevisiae

2004 ◽  
Vol 15 (5) ◽  
pp. 2189-2204 ◽  
Author(s):  
Fulvio Reggiori ◽  
Chao-Wen Wang ◽  
Usha Nair ◽  
Takahiro Shintani ◽  
Hagai Abeliovich ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Secretory Pathway ◽  
Membrane Vesicle ◽  
Endomembrane System ◽  
Vesicle Membrane ◽  
Double Membrane ◽  
Vesicle Biogenesis ◽  
Molecular Components ◽  
Vacuolar Trafficking

The Cvt pathway is a biosynthetic transport route for a distinct subset of resident yeast vacuolar hydrolases, whereas macroautophagy is a nonspecific degradative mechanism that allows cell survival during starvation. Yet, these two vacuolar trafficking pathways share a number of identical molecular components and are morphologically very similar. For example, one of the hallmarks of both pathways is the formation of double-membrane cytosolic vesicles that sequester cargo before vacuolar delivery. The origin of the vesicle membrane has been controversial and various lines of evidence have implicated essentially all compartments of the endomembrane system. Despite the analogies between the Cvt pathway and autophagy, earlier work has suggested that the origin of the engulfing vesicle membranes is different; the endoplasmic reticulum is proposed to be required only for autophagy. In contrast, in this study we demonstrate that the endoplasmic reticulum and/or Golgi complex, but not endosomal compartments, play an important role for both yeast transport routes. Along these lines, we demonstrate that Berkeley bodies, a structure generated from the Golgi complex in sec7 cells, are immunolabeled with Atg8, a structural component of autophagosomes. Finally, we also show that none of the yeast t-SNAREs are located at the preautophagosomal structure, the presumed site of double-membrane vesicle formation. Based on our results, we propose two models for Cvt vesicle biogenesis.

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