scholarly journals Oligosaccharide-based Information in Endoplasmic Reticulum Quality Control and Other Biological Systems

2001 ◽  
Vol 276 (12) ◽  
pp. 8623-8626 ◽  
Author(s):  
Mark A. Lehrman
Keyword(s):  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Biological Systems ◽  
Endoplasmic Reticulum Quality Control

scholarly journals Mechanism of Class 1 (Glycosylhydrolase Family 47) α-Mannosidases Involved inN-Glycan Processing and Endoplasmic Reticulum Quality Control

2005 ◽  
Vol 280 (16) ◽  
pp. 16197-16207 ◽  
Author(s):  
Khanita Karaveg ◽  
Aloysius Siriwardena ◽  
Wolfram Tempel ◽  
Zhi-Jie Liu ◽  
John Glushka ◽  
...  
Keyword(s):  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Bond Cleavage ◽  
Substrate Analog ◽  
Acid And Base ◽  
Class 1 ◽  
Glycoside Bond ◽  
Endoplasmic Reticulum Quality Control ◽  
Mutant Forms ◽  
Hydrolytic Mechanism

Quality control in the endoplasmic reticulum (ER) determines the fate of newly synthesized glycoproteins toward either correct folding or disposal by ER-associated degradation. Initiation of the disposal process involves selective trimming ofN-glycans attached to misfolded glycoproteins by ER α-mannosidase I and subsequent recognition by the ER degradation-enhancing α-mannosidase-like protein family of lectins, both members of glycosylhydrolase family 47. The unusual inverting hydrolytic mechanism catalyzed by members of this family is investigated here by a combination of kinetic and binding analyses of wild type and mutant forms of human ER α-mannosidase I as well as by structural analysis of a co-complex with an uncleaved thiodisaccharide substrate analog. These data reveal the roles of potential catalytic acid and base residues and the identification of a novel3S1sugar conformation for the bound substrate analog. The co-crystal structure described here, in combination with the1C4conformation of a previously identified co-complex with the glycone mimic, 1-deoxymannojirimycin, indicates that glycoside bond cleavage proceeds through a least motion conformational twist of a properly predisposed substrate in the –1 subsite. A novel3H4conformation is proposed as the exploded transition state.

scholarly journals Crystal structure of a class I α1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control

2000 ◽  
Vol 19 (4) ◽  
pp. 581-588 ◽  
Author(s):  
François Vallée ◽  
Francesco Lipari ◽  
Patrick Yip ◽  
Barry Sleno ◽  
Annette Herscovics ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Class I ◽  
Endoplasmic Reticulum Quality Control

scholarly journals Sorting things out through endoplasmic reticulum quality control

2010 ◽  
Vol 27 (8) ◽  
pp. 412-427 ◽  
Author(s):  
Taku Tamura ◽  
Johan C. Sunryd ◽  
Daniel N. Hebert
Keyword(s):  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Quality Control

scholarly journals Endoplasmic reticulum quality control regulates the fate of transthyretin variants in the cell

2007 ◽  
Vol 26 (10) ◽  
pp. 2501-2512 ◽  
Author(s):  
Takashi Sato ◽  
Seiko Susuki ◽  
Mary Ann Suico ◽  
Masanori Miyata ◽  
Yukio Ando ◽  
...  
Keyword(s):  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Quality Control

scholarly journals Brucella effector hijacks endoplasmic reticulum quality control machinery to prevent premature egress

2019 ◽  
Author(s):  
Jean-Baptiste Luizet ◽  
Julie Raymond ◽  
Thais Lourdes Santos Lacerda ◽  
Magali Bonici ◽  
Frédérique Lembo ◽  
...  
Keyword(s):  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Er Quality Control ◽  
Unfolded Protein ◽  
Type Iv ◽  
Endoplasmic Reticulum Quality Control ◽  
Fine Regulation ◽  
Infected Cells ◽  
The Unfolded Protein Response ◽  
Protein Response

AbstractPerturbation of endoplasmic reticulum (ER) functions can have critical consequences for cellular homeostasis. An elaborate surveillance system known as ER quality control (ERQC) ensures that only correctly assembled proteins reach their destination. Persistence of misfolded or improperly matured proteins upregulates the unfolded protein response (UPR) to cope with stress, activates ER associated degradation (ERAD) for delivery to proteasomes for degradation. We have identified a Brucella abortus type IV secretion system effector called BspL that targets Herp, a key component of ERQC and is able to augment ERAD. Modulation of ERQC by BspL results in tight control of the kinetics of autophagic Brucella-containing vacuole formation, preventing premature bacterial egress from infected cells. This study highlights how bacterial pathogens may hijack ERAD components for fine regulation of their intracellular trafficking.

scholarly journals Endoplasmic reticulum quality control of LDLR variants associated with familial hypercholesterolemia

FEBS Open Bio ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 1994-2005 ◽  
Author(s):  
Praseetha Kizhakkedath ◽  
Anne John ◽  
Buthaina K. Al‐Sawafi ◽  
Lihadh Al‐Gazali ◽  
Bassam R. Ali
Keyword(s):  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Familial Hypercholesterolemia ◽  
Endoplasmic Reticulum Quality Control
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