Fbs2 Is a New Member of the E3 Ubiquitin Ligase Family That Recognizes Sugar Chains

Yoshida, Yasuko; Tokunaga, Fuminori; Chiba, Tomoki; Iwaï, Kazuhiro; Tanaka, Keiji; Tai, Tadashi

doi:10.1074/jbc.m304157200

Cited by 168 publications

(128 citation statements)

References 33 publications

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“…We previously found that glycosylated H2a is a substrate for two E3 ubiquitin ligases, HRD1 and SCF Fbs2 (13). The latter carries the substrate-recognition subunit Fbs2, which possesses a high mannose glycan binding domain (35). H2a⌬gly and WT H2a showed similar association with HRD1 (Fig.…”

Section: Components Of the Glycoprotein Erad Pathway Target A Nonglycmentioning

confidence: 93%

A Shared Endoplasmic Reticulum-associated Degradation Pathway Involving the EDEM1 Protein for Glycosylated and Nonglycosylated Proteins

Shenkman

Groisman

Ron

et al. 2013

Journal of Biological Chemistry

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Background: N-Glycan processing and interactions with lectins regulate the quality control and endoplasmic reticulumassociated degradation (ERAD) of glycoproteins. Results: Most of the same machinery targets nonglycosylated misfolded proteins. Conclusion: They share some membrane and luminal ERAD machinery but not all cytosolic components. Significance: ER glycan-interacting proteins must possess a dual specificity for glycan structure and for exposed misfolded polypeptide domains.

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Section: Components Of the Glycoprotein Erad Pathway Target A Nonglycmentioning

confidence: 93%

A Shared Endoplasmic Reticulum-associated Degradation Pathway Involving the EDEM1 Protein for Glycosylated and Nonglycosylated Proteins

Shenkman

Groisman

Ron

et al. 2013

Journal of Biological Chemistry

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“…Fbs1 is an F-box protein, a component of the SCF E3 ubiquitin ligase, which is composed of the Skp1, Cul1, Roc1͞Rbx1, and F-box proteins (15). The F-box proteins are the substrate-binding components of this E3 complex, and in the case of Fbs1, it was shown to recognize N-linked glycans, especially the chitobiose core via its sugar-binding domain (16,17).…”

Section: Resultsmentioning

confidence: 99%

Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannose-binding module

Zhou

Zhao

Truglio

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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The inability of certain N-linked glycoproteins to adopt their native conformation in the endoplasmic reticulum (ER) leads to their retrotranslocation into the cytosol and subsequent degradation by the proteasome. In this pathway the cytosolic peptide-N-glycanase (PNGase) cleaves the N-linked glycan chains off denatured glycoproteins. PNGase is highly conserved in eukaryotes and plays an important role in ER-associated protein degradation. In higher eukaryotes, PNGase has an N-terminal and a C-terminal extension in addition to its central catalytic domain, which is structurally and functionally related to transglutaminases. Although the N-terminal domain of PNGase is involved in protein-protein interactions, the function of the C-terminal domain has not previously been characterized. Here, we describe biophysical, biochemical, and crystallographic studies of the mouse PNGase C-terminal domain, including visualization of a complex between this domain and mannopentaose. These studies demonstrate that the C-terminal domain binds to the mannose moieties of N-linked oligosaccharide chains, and we further show that it enhances the activity of the mouse PNGase core domain, presumably by increasing the affinity of mouse PNGase for the glycan chains of misfolded glycoproteins.endoplasmic reticulum ͉ N-linked glycoproteins ͉ proteasome ͉ protein degradation ͉ deglycosylation

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“…Ubiquitination of αTCR is mediated by at least two different ubiquitin ligases (E3s): cytosolic SCF Fbs1,2 which recognizes N-linked oligosaccharides attached to dislocated αTCR chain [13] and ER-membrane associated HRD1 [14]. Degradation of other TCR subunits bears important mechanistic differences from the degradation of αTCR.…”

Section: Introductionmentioning

confidence: 99%

A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum

Lass

McConnell

Nowis

et al. 2007

Archives of Biochemistry and Biophysics

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Summaryα chain of T-cell receptor (TCR) is a typical ERAD (ER-associated degradation) substrate degraded in the absence of other TCR subunits. Depletion of derlin1 fails to induce accumulation of αTCR despite inducing accumulation of α1-antitrypsin, another ERAD substrate. Furthermore, while depletion of VCP does not affect levels of α1-antitrypsin, it induces an increase in levels of αTCR. RNAi of VCP induces preferential accumulation of αTCR with less mannose residues, suggesting its retention within the ER. Mass spectrometric analysis of cellular N-linked glycans revealed that depletion of VCP decreases the level of high mannose glycoproteins, increases the levels of truncated low-mannose glycoproteins and induces changes in the abundance of complex glycans assembled in post-ER compartments. Since proteasome inhibition was unable to mimic those changes, they can not be regarded as a simple consequence of inhibited ERAD but represent a complex effect of VCP on the function of the ER.

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Fbs2 Is a New Member of the E3 Ubiquitin Ligase Family That Recognizes Sugar Chains

Cited by 168 publications

References 33 publications

A Shared Endoplasmic Reticulum-associated Degradation Pathway Involving the EDEM1 Protein for Glycosylated and Nonglycosylated Proteins

A Shared Endoplasmic Reticulum-associated Degradation Pathway Involving the EDEM1 Protein for Glycosylated and Nonglycosylated Proteins

Structural and biochemical studies of the C-terminal domain of mouse peptide-N-glycanase identify it as a mannose-binding module

A novel function of VCP (valosin-containing protein; p97) in the control of N-glycosylation of proteins in the endoplasmic reticulum

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