Endoplasmic Reticulum-Associated Degradation of Cytochrome P450 CYP3A4 in Saccharomyces cerevisiae: Further Characterization of Cellular Participants and Structural Determinants

2006 ◽  
Vol 69 (6) ◽  
pp. 1897-1904 ◽  
Author(s):  
Mingxiang Liao ◽  
Saadia Faouzi ◽  
Andrey Karyakin ◽  
Maria Almira Correia
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Cytochrome P450 ◽  
Structural Determinants ◽  
Endoplasmic Reticulum Associated Degradation

scholarly journals Immunoisolaton of the Yeast Golgi Subcompartments and Characterization of a Novel Membrane Protein, Svp26, Discovered in the Sed5-Containing Compartments

2005 ◽  
Vol 25 (17) ◽  
pp. 7696-7710 ◽  
Author(s):  
Hironori Inadome ◽  
Yoichi Noda ◽  
Hiroyuki Adachi ◽  
Koji Yoda
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Membrane Proteins ◽  
Golgi Apparatus ◽  
Membrane Protein ◽  
Considerable Portion ◽  
Marker Proteins ◽  
Evolutionarily Conserved ◽  
Golgi Compartment

ABSTRACT The Golgi apparatus consists of a set of vesicular compartments which are distinguished by their marker proteins. These compartments are physically separated in the Saccharomyces cerevisiae cell. To characterize them extensively, we immunoisolated vesicles carrying either of the SNAREs Sed5 or Tlg2, the markers of the early and late Golgi compartments, respectively, and analyzed the membrane proteins. The composition of proteins was mostly consistent with the position of each compartment in the traffic. We found six uncharacterized but evolutionarily conserved proteins and named them Svp26 (Sed5 compartment vesicle protein of 26 kDa), Tvp38, Tvp23, Tvp18, Tvp15 (Tlg2 compartment vesicle proteins of 38, 23, 18, and 15 kDa), and Gvp36 (Golgi vesicle protein of 36 kDa). The localization of Svp26 in the early Golgi compartment was confirmed by microscopic and biochemical means. Immunoprecipitation indicated that Svp26 binds to itself and a Golgi mannosyltransferase, Ktr3. In the absence of Svp26, a considerable portion of Ktr3 was mislocalized in the endoplasmic reticulum. Our data suggest that Svp26 has a novel role in retention of a subset of membrane proteins in the early Golgi compartments.

scholarly journals Characterization of protein complexes of the endoplasmic reticulum-associated degradation E3 ubiquitin ligase Hrd1

2017 ◽  
Vol 292 (22) ◽  
pp. 9104-9116 ◽  
Author(s):  
Jiwon Hwang ◽  
Christopher P. Walczak ◽  
Thomas A. Shaler ◽  
James A. Olzmann ◽  
Lichao Zhang ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Ubiquitin Ligase ◽  
Protein Complexes ◽  
E3 Ubiquitin Ligase ◽  
Endoplasmic Reticulum Associated Degradation

scholarly journals Liver Cytochrome P450 3A Endoplasmic Reticulum-associated Degradation

2010 ◽  
Vol 286 (5) ◽  
pp. 3815-3828 ◽  
Author(s):  
Poulomi Acharya ◽  
Mingxiang Liao ◽  
Juan C. Engel ◽  
Maria Almira Correia
Keyword(s):  
Endoplasmic Reticulum ◽  
Cytochrome P450 ◽  
Cytochrome P450 3A ◽  
Liver Cytochrome ◽  
Endoplasmic Reticulum Associated Degradation

scholarly journals ERS-24, a Mammalian v-SNARE Implicated in Vesicle Traffic between the ER and the Golgi

1997 ◽  
Vol 137 (5) ◽  
pp. 1017-1028 ◽  
Author(s):  
Inbok Paek ◽  
Lelio Orci ◽  
Mariella Ravazzola ◽  
Hediye Erdjument-Bromage ◽  
Mylene Amherdt ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Sequence Homology ◽  
Vesicular Transport ◽  
Dependent Manner ◽  
Vesicle Traffic ◽  
Transport Vesicles ◽  
Identification And Characterization

We report the identification and characterization of ERS-24 (Endoplasmic Reticulum SNARE of 24 kD), a new mammalian v-SNARE implicated in vesicular transport between the ER and the Golgi. ERS24 is incorporated into 20S docking and fusion particles and disassembles from this complex in an ATP-dependent manner. ERS-24 has significant sequence homology to Sec22p, a v-SNARE in Saccharomyces cerevisiae required for transport between the ER and the Golgi. ERS-24 is localized to the ER and to the Golgi, and it is enriched in transport vesicles associated with these organelles.

scholarly journals Investigating the role of ERAD on antibody processing in glycoengineered Saccharomyces cerevisiae

2020 ◽  
Vol 20 (1) ◽  
Author(s):  
Mari A Piirainen ◽  
Alexander D Frey
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Heavy Chain ◽  
Chain Molecules ◽  
Secretion Signal ◽  
Endoplasmic Reticulum Associated Degradation ◽  
Endoplasmic Reticulum Quality Control ◽  
Therapeutic Glycoproteins

ABSTRACT N-glycosylation plays an important role in the endoplasmic reticulum quality control (ERQC). N-glycan biosynthesis pathways have been engineered in yeasts and fungi to enable the production of therapeutic glycoproteins with human-compatible N-glycosylation, and some glycoengineering approaches alter the synthesis of the lipid-linked oligosaccharide (LLO). Because the effects of LLO engineering on ERQC are currently unknown, we characterized intracellular processing of IgG in glycoengineered Δalg3 Δalg11 Saccharomyces cerevisiae strain and analyzed how altered LLO structures affect endoplasmic reticulum-associated degradation (ERAD). Intracellular IgG light and heavy chain molecules expressed in Δalg3 Δalg11 strain are ERAD substrates and targeted to ERAD independently of Yos9p and Htm1p, whereas in the presence of ALG3 ERAD targeting is dependent on Yos9p but does not require Htm1p. Blocking of ERAD accumulated ER and post-Golgi forms of IgG and increased glycosylation of matα secretion signal but did not improve IgG secretion. Our results show ERAD targeting of a heterologous glycoprotein in yeast, and suggest that proteins in the ER can be targeted to ERAD via other mechanisms than the Htm1p-Yos9p-dependent route when the LLO biosynthesis is altered.

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