Association of malectin with ribophorin I is crucial for attenuation of misfolded glycoprotein secretion

Takeda, Koh; Qin, Sheng-Ying; Matsumoto, Naoki; Yamamoto, Kazuo

doi:10.1016/j.bbrc.2014.10.102

Cited by 33 publications

(31 citation statements)

References 18 publications

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“…3c). A truncated malectin derivative that does not bind ribophorin I does not reduce AT NHK secretion [21]. The preferential association of malectin with AT NHK or misfolded HA conformers has led to the hypothesis that a malectin-glycan interaction can pre-emptively divert proteins into the ERAD pathway [18,19].…”

Section: Metazoan Cells Express Two Oligosaccharyltransferase Complexesmentioning

confidence: 99%

N-linked glycosylation and homeostasis of the endoplasmic reticulum

Cherepanova

Shrimal

Gilmore

2016

Current Opinion in Cell Biology

214

217

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Summary As a major site of protein biosynthesis, homeostasis of the endoplasmic reticulum is critical for cell viability. Asparagine linked glycosylation of newly synthesized proteins by the oligosaccharyltransferase plays a central role in ER homeostasis due to the use of protein-linked oligosaccharides as recognition and timing markers for glycoprotein quality control pathways that discriminate between correctly folded proteins and terminally malfolded proteins destined for ER associated degradation. Recent findings indicate how the oligosaccharyltransferase achieves efficient and accurate glycosylation of the diverse proteins that enter the endoplasmic reticulum. In metazoan organisms two distinct OST complexes cooperate to maximize the glycosylation of nascent proteins. The STT3B complex glycosylates acceptor sites that have been skipped by the translocation channel associated STT3A complex.

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Section: Metazoan Cells Express Two Oligosaccharyltransferase Complexesmentioning

confidence: 99%

N-linked glycosylation and homeostasis of the endoplasmic reticulum

Cherepanova

Shrimal

Gilmore

2016

Current Opinion in Cell Biology

214

217

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“…RLKs constitute a gene subfamily of over 600 members in Arabidopsis (Shiu and Bleecker, 2001a,b, 2003). Malectin is a membrane-anchored protein of the endoplasmic reticulum that recognizes and binds to Glc2-N-glycan, thereby regulating the production and secretion of N -glycosylated proteins (Schallus et al, 2008, 2010; Takeda et al, 2014). Interestingly, a group of RLKs harbors an extracellular sequence with a unique domain that is similar to malectin (Schulze-Muth et al, 1996; Boisson-Dernier et al, 2011; Lindner et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

A FERONIA-Like Receptor Kinase Regulates Strawberry (Fragaria × ananassa) Fruit Ripening and Quality Formation

et al. 2017

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Ripening of fleshy fruits is controlled by a series of intricate signaling processes. Here, we report a FERONIA/FER-like receptor kinase, FaMRLK47, that regulates both strawberry (Fragaria × ananassa) fruit ripening and quality formation. Overexpression and RNAi-mediated downregulation of FaMRLK47 delayed and accelerated fruit ripening, respectively. We showed that FaMRLK47 physically interacts with FaABI1, a negative regulator of abscisic acid (ABA) signaling, and demonstrated that FaMRLK47 regulates fruit ripening by modulating ABA signaling, a major pathway governing strawberry fruit ripening. In accordance with these findings, overexpression and RNAi-mediated downregulation of FaMRLK47 caused a decrease and increase, respectively, in the ABA-induced expression of a series of ripening-related genes. Additionally, overexpression and RNAi-mediated downregulation of FaMRLK47 resulted in an increase and decrease in sucrose content, respectively, as compared with control fruits, and respectively promoted and inhibited the expression of genes in the sucrose biosynthesis pathway (FaSS and FaSPS). Collectively, this study demonstrates that FaMRLK47 is an important regulator of strawberry fruit ripening and quality formation, and sheds light on the signaling mechanisms underlying strawberry fruit development and ripening.

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“…The OST-B complex also binds malectin, but with a higher affinity than OST-A. Malectin, in association with ribophorin I, preferentially associates with the misfolded glycoproteins and guides these to the proteasome for degradation [86,87]. Thus, malectin is involved in the quality control of glycoproteins in the ER [87].…”

Section: Humanmentioning

confidence: 99%

“…Malectin, in association with ribophorin I, preferentially associates with the misfolded glycoproteins and guides these to the proteasome for degradation [86,87]. Thus, malectin is involved in the quality control of glycoproteins in the ER [87]. Since unfolded glycoproteins increase the interaction between malectin and ribophorin I [88], this suggests that the OST-B complex may encounter more unfolded glycoproteins than OST-A.…”

Section: Humanmentioning

confidence: 99%

Structural Insight into the Mechanism of N-Linked Glycosylation by Oligosaccharyltransferase

2020

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Asparagine-linked glycosylation, also known as N-linked glycosylation is an essential and highly conserved post-translational protein modification that occurs in all three domains of life. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell–cell communication, and stability. Defects in N-linked glycosylation results in a class of inherited diseases known as congenital disorders of glycosylation (CDG). N-linked glycosylation occurs in the endoplasmic reticulum (ER) lumen by a membrane associated enzyme complex called the oligosaccharyltransferase (OST). In the central step of this reaction, an oligosaccharide group is transferred from a lipid-linked dolichol pyrophosphate donor to the acceptor substrate, the side chain of a specific asparagine residue of a newly synthesized protein. The prokaryotic OST enzyme consists of a single polypeptide chain, also known as single subunit OST or ssOST. In contrast, the eukaryotic OST is a complex of multiple non-identical subunits. In this review, we will discuss the biochemical and structural characterization of the prokaryotic, yeast, and mammalian OST enzymes. This review explains the most recent high-resolution structures of OST determined thus far and the mechanistic implication of N-linked glycosylation throughout all domains of life. It has been shown that the ssOST enzyme, AglB protein of the archaeon Archaeoglobus fulgidus, and the PglB protein of the bacterium Campylobactor lari are structurally and functionally similar to the catalytic Stt3 subunit of the eukaryotic OST enzyme complex. Yeast OST enzyme complex contains a single Stt3 subunit, whereas the human OST complex is formed with either STT3A or STT3B, two paralogues of Stt3. Both human OST complexes, OST-A (with STT3A) and OST-B (containing STT3B), are involved in the N-linked glycosylation of proteins in the ER. The cryo-EM structures of both human OST-A and OST-B complexes were reported recently. An acceptor peptide and a donor substrate (dolichylphosphate) were observed to be bound to the OST-B complex whereas only dolichylphosphate was bound to the OST-A complex suggesting disparate affinities of two OST complexes for the acceptor substrates. However, we still lack an understanding of the independent role of each eukaryotic OST subunit in N-linked glycosylation or in the stabilization of the enzyme complex. Discerning the role of each subunit through structure and function studies will potentially reveal the mechanistic details of N-linked glycosylation in higher organisms. Thus, getting an insight into the requirement of multiple non-identical subunits in the N-linked glycosylation process in eukaryotes poses an important future goal.

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Association of malectin with ribophorin I is crucial for attenuation of misfolded glycoprotein secretion

Cited by 33 publications

References 18 publications

N-linked glycosylation and homeostasis of the endoplasmic reticulum

N-linked glycosylation and homeostasis of the endoplasmic reticulum

A FERONIA-Like Receptor Kinase Regulates Strawberry (Fragaria × ananassa) Fruit Ripening and Quality Formation

Structural Insight into the Mechanism of N-Linked Glycosylation by Oligosaccharyltransferase

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