N-linked glycan recognition and processing: the molecular basis of endoplasmic reticulum quality control

Moremen, Kelley W.; Molinari, Maurizio

doi:10.1016/j.sbi.2006.08.005

Cited by 119 publications

(87 citation statements)

References 49 publications

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“…In particular, protein glycans are recognition signals for the entry to and exit from the ER protein folding apparatus involving calnexin (CNX) and calreticulin (CRT). Many reviews have been written on the subject, including Helenius and Aebi (2004), Moremen and Molinari (2006), Caramelo and Parodi (2008), and a recent article about CRT in plants (Jia et al, 2009). Two N-acetylglucosamine (N1 and N2, gray squares) and five mannose residues (M3 to M7, gray, pink, and blue circles) are added subsequently to the polyisoprenoid lipid dolichol (Dol) on the cytoplasmic side of the ER.…”

Section: Protein N-glycosylationmentioning

confidence: 99%

Endoplasmic Reticulum Protein Quality Control and Its Relationship to Environmental Stress Responses in Plants

2010

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The endoplasmic reticulum (ER) has a sophisticated quality control (QC) system to eliminate improperly folded proteins from the secretory pathway. Given that protein folding is such a fastidious process and subject to adverse environmental conditions, the ER QC system appears to have been usurped to serve as an environmental sensor and responder in plants. Under stressful conditions, the ER protein folding machinery reaches a limit as the demands for protein folding exceed the capacity of the system. Under these conditions, misfolded or unfolded proteins accumulate in the ER, triggering an unfolded protein response (UPR). UPR mitigates ER stress by upregulating the expression of genes encoding components of the protein folding machinery or the ER-associated degradation system. In Arabidopsis thaliana, ER stress is sensed and stress signals are transduced by membrane-bound transcription factors, which are activated and mobilized under environmental stress conditions. Under acute or chronic stress conditions, UPR can also lead to apoptosis or programmed cell death. Despite recent progress in our understanding of plant protein QC, discovering how different environmental conditions are perceived is one of the major challenges in understanding this system. Since the ER QC system is one among many stress response systems in plants, another major challenge is determining the extent to which the ER QC system contributes to various stress responses in plants.

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Section: Protein N-glycosylationmentioning

confidence: 99%

Endoplasmic Reticulum Protein Quality Control and Its Relationship to Environmental Stress Responses in Plants

2010

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“…Calnexin has been implicated in several genetic diseases caused by inherited protein folding defects (Amaral, 2004;Chevet et al, 1999;Kuznetsov and Nigam, 1998;Ni and Lee, 2007). Mechanistically, calnexin interacts with nascent polypeptides as a lectin that binds N-linked glycan, and/or via protein-protein contacts (Bedard et al, 2005;Caramelo and Parodi, 2008;Helenius and Aebi, 2004;Marechal et al, 2004;Moremen and Molinari, 2006;Thammavongsa et al, 2005;Williams, 2006).…”

Section: Introductionmentioning

confidence: 99%

A nucleolar protein allows viability in the absence of the essential ER-residing molecular chaperone calnexin

Beauregard

Guérin

Turcotte

et al. 2009

Journal of Cell Science

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In fission yeast, the ER-residing molecular chaperone calnexin is normally essential for viability. However, a specific mutant of calnexin that is devoid of chaperone function (Δhcd_Cnx1p) induces an epigenetic state that allows growth of Schizosaccharomyces pombe without calnexin. This calnexin-independent (Cin) state was previously shown to be mediated via a non-chromosomal element exhibiting some prion-like features. Here, we report the identification of a gene whose overexpression induces the appearance of stable Cin cells. This gene, here named cif1+ for calnexin-independence factor 1, encodes an uncharacterized nucleolar protein. The Cin cells arising from cif1+ overexpression (Cincif1 cells) are genetically and phenotypically distinct from the previously characterized CinΔhcd_cnx1 cells, which spontaneously appear in the presence of the Δhcd_Cnx1p mutant. Moreover, cif1+ is not required for the induction or maintenance of the CinΔhcd_cnx1 state. These observations argue for different pathways of induction and/or maintenance of the state of calnexin independence. Nucleolar localization of Cif1p is required to induce the Cincif1 state, thus suggesting an unexpected interaction between the vital cellular role of calnexin and a function of the nucleolus.

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“…The possibility has been suggested that they are partially rescued by BiP, suggesting the presence of a fail-safe mechanism in the system in ER. 37) II. Functional Analysis of Glycoprotein Glycans by Using Chemically Synthesized Probes…”

Section: Biosynthesis and Processing Of N-glycosylated Proteins Anmentioning

confidence: 99%

Deciphering the Roles of Glycan Processing in Glycoprotein Quality Control through Organic Synthesis

Ito

Takeda

2013

Bioscience, Biotechnology, and Biochemistry

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N-linked glycan recognition and processing: the molecular basis of endoplasmic reticulum quality control

Cited by 119 publications

References 49 publications

Endoplasmic Reticulum Protein Quality Control and Its Relationship to Environmental Stress Responses in Plants

Endoplasmic Reticulum Protein Quality Control and Its Relationship to Environmental Stress Responses in Plants

A nucleolar protein allows viability in the absence of the essential ER-residing molecular chaperone calnexin

Deciphering the Roles of Glycan Processing in Glycoprotein Quality Control through Organic Synthesis

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