Clusters of VIP36-Positive Vesicles between Endoplasmic Reticulum and Golgi Apparatus in GH3 Cells

Shimada, Osamu; Hara-Kuge, Sayuri; Yamashita, Katsuko; Tosaka-Shimada, Hisami; Li, Yanchao; Li, Yongnan; Atsumi, Saoko; Ishikawa, Harunori

doi:10.1247/csf.28.155

Cited by 11 publications

(7 citation statements)

References 34 publications

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“…8). The interactions of N-linked carbohydrates of CFTR at the ER might not be limited to these two chaperones, but could also involve lectin receptors such as ERGIC53 (LMAN1), VIP36 (LMAN2), VIPL (LMAN2L) or erlectin, which have all been shown to facilitate trafficking of certain glycoproteins in the early secretory pathway (Appenzeller-Herzog and Hauri, 2006; Appenzeller et al, 1999; Cruciat et al, 2006; Neve et al, 2003; Shimada et al, 2003). …”

Section: Discussionmentioning

confidence: 99%

Role of N-linked oligosaccharides in the biosynthetic processing of the cystic fibrosis membrane conductance regulator

Chang

Mengos

Hou

et al. 2008

Journal of Cell Science

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Section: Discussionmentioning

confidence: 99%

Role of N-linked oligosaccharides in the biosynthetic processing of the cystic fibrosis membrane conductance regulator

Chang

Mengos

Hou

et al. 2008

Journal of Cell Science

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“…If properly folded, it moves to the Golgi. Exit from the ER may be assisted by mannose-binding lectins, such as ERGIC-53, VIP36, and VIPL (2,62,83). If the glycoprotein is incompletely folded, it becomes a substrate for a luminal ER glucosyltransferase that reglucosylates the glycans located in improperly folded regions.…”

Section: Role Of N-glycans In Protein Folding Stability and Qualitymentioning

confidence: 99%

“…One potential apical sorting receptor, the mannose-binding lectin VIP36 (43,44,79), is predominantly localized in ERGIC and the cis-Golgi (36,83), and to a lesser extent in the TGN and plasma membrane (34,82). VIP36 plays a role in the export of glycoproteins from the ER (36,83) (Table 2).…”

Section: Putative Apical Sorting Machinery That Recognizes N-glycansmentioning

confidence: 99%

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Role of N-glycosylation in trafficking of apical membrane proteins in epithelia

Vagin

Kraut²,

Sachs³

2009

American Journal of Physiology-Renal Physiology

178

157

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ized distribution of plasma membrane transporters and receptors in epithelia is essential for vectorial functions of epithelia. This polarity is maintained by sorting of membrane proteins into apical or basolateral transport containers in the transGolgi network and/or endosomes followed by their delivery to the appropriate plasma membrane domains. Sorting depends on the recognition of sorting signals in proteins by specific sorting machinery. In the present review, we summarize experimental evidence for and against the hypothesis that N-glycans attached to the membrane proteins can act as apical sorting signals. Furthermore, we discuss the roles of N-glycans in the apical sorting event per se and their contribution to folding and quality control of glycoproteins in the endoplasmic reticulum or retention of glycoproteins in the plasma membrane. Finally, we review existing hypotheses on the mechanism of apical sorting and discuss the potential roles of the lectins, VIP36 and galectin-3, as putative apical sorting receptors. apical sorting; apical membrane retention; H-K-ATPase ␤-subunit; lectin EPITHELIAL CELLS CARRY OUT vectorial transport that requires polarized distribution of transporters and receptors to apical or basolateral membrane domains. These domains are separated by tight junctions that connect neighboring cells in the epithelial monolayer and act as diffusion barriers to prevent mixing of apical and basolateral membrane components (22). Asymmetric distribution of plasma membrane proteins is accomplished by their sorting into apical and basolateral containers in the trans-Golgi network (TGN) and/or endosomes followed by vectorial transport of these containers and insertion and retention of the proteins in the appropriate plasma membrane domains. Sorting depends on recognition of apical and basolateral sorting signals within the proteins by cellular sorting machinery (20,58,59,75,76).Numerous studies have indicated that both O-and N-glycans attached to the extracellular domains of some membrane proteins are important for apical location of these proteins. This review will focus on the role of N-glycans in polarized distribution of plasma membrane proteins in epithelia. The role of O-glycans in apical sorting has been described in several recent excellent reviews (18, 71) and will not be discussed further here.A putative role of N-glycans as apical sorting signals was postulated more than 10 years ago (24, 31). However, this hypothesis remains controversial primarily because N-glycans are important for the processes that precede or follow the actual sorting event, such as protein folding, quality control, endoplasmic reticulum (ER)-associated degradation, ER-to-Golgi trafficking, and retention of glycoproteins in the apical membrane. Therefore, merely examining the effect of altering the number or the nature of N-linked glycans on the relative abundance of the glycoprotein in the apical membrane, as has been done in many of the studies reported, does not allow one to distinguish between effects on apica...

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“…20) VIP36 shares significant homology with leguminous lectins, and its broad localization from the ER to the Golgi [21][22][23] indicates that VIP36 functions as a cargo receptor that transports various glycoproteins. It is believed to participate not only in the export of folded proteins from the ER, but also in the retrieval of misfolded proteins from the Golgi to the ER (Fig.…”

Section: Structures and Sugar-binding Specifici-ties Of Intracellularmentioning

confidence: 99%

Intracellular Lectins Involved in Folding and Transport in the Endoplasmic Reticulum

Yamamoto

2009

Biological & Pharmaceutical Bulletin

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Glycosylation is a highly sophisticated post-translational modification of proteins that occurs in the endoplasmic reticulum (ER) and the Golgi apparatus. The vital biological functions served by protein glycosylation can be separated into two types. The first is the role of glycosylation in the extracellular environment, where a variety of sugar chains participate in protein secretion and stability, cell-cell adhesion and signaling, innate immunity, embryogenesis, and morphogenesis. Another role is in quality control of glycoproteins in the ER, a topic that has received recent attention. Quality control of glycoproteins is categorized into three kinds of reactions; the first is folding of newly synthesized glycoproteins, the second is ER-associated degradation of terminally misfolded or unassembled glycoproteins, and the last is sorting and transport of glycoproteins between organelles. In all three processes, N-glycans on the glycoproteins are used as tags to initiate the reactions. The process of glycosylation is conserved in yeast, plants, invertebrates and vertebrates, including mammals. Here, I focus on the intracellular lectins that participate in these processes and discuss the role of glycosylation based on the structural differences of N-glycans.

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Clusters of VIP36-Positive Vesicles between Endoplasmic Reticulum and Golgi Apparatus in GH3 Cells

Cited by 11 publications

References 34 publications

Role of N-linked oligosaccharides in the biosynthetic processing of the cystic fibrosis membrane conductance regulator

Role of N-linked oligosaccharides in the biosynthetic processing of the cystic fibrosis membrane conductance regulator

Role of N-glycosylation in trafficking of apical membrane proteins in epithelia

Intracellular Lectins Involved in Folding and Transport in the Endoplasmic Reticulum

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