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Lectin, mannose-binding 2

VIP36, vesicular integral protein of 36 kDa
This gene encodes a type I transmembrane lectin that shuttles between the endoplasmic reticulum, the Golgi apparatus and the plasma membrane. The encoded protein binds high mannose type glycoproteins and may facilitate their sorting, trafficking and quality control. [provided by RefSeq, Oct 2008] (from NCBI)
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Top mentioned proteins: ERGIC-53, CD45, CAN, Endo, calreticulin
Papers on VIP36
Modulating endoplasmic reticulum-Golgi cargo receptors for improving secretion of carrier-fused heterologous proteins in the filamentous fungus Aspergillus oryzae.
Kitamoto et al., Tokyo, Japan. In Appl Environ Microbiol, 2015
Here, using Aspergillus oryzae as a model filamentous fungus, we studied the involvement of two putative lectin-like cargo receptors, A. oryzae Vip36 (AoVip36) and AoEmp47, in the secretion of heterologous proteins expressed in fusion with the endogenous enzyme α-amylase as the carrier.
Cloning and characterization of two different L-type lectin genes from the Chinese mitten crab Eriocheir sinensis.
Ren et al., Nanjing, China. In Dev Comp Immunol, 2014
The full-length cDNA of VIP36 was 3474 bp with a 984 bp ORF encoding a 327-amino acid peptide.
Structural basis for disparate sugar-binding specificities in the homologous cargo receptors ERGIC-53 and VIP36.
Kato et al., Nagoya, Japan. In Plos One, 2013
ERGIC-53 and VIP36 are categorized as leguminous type (L-type) lectins, and they function as cargo receptors for trafficking certain N-linked glycoproteins in the secretory pathway in animal cells.
Parallel quantification of lectin-glycan interaction using ultrafiltration.
Ito et al., Wako, Japan. In Carbohydr Res, 2013
Estimated Ka values of malectin and VIP36 were in good agreement indeed with those evaluated by conventional methods such as isothermal titration calorimetry (ITC) or frontal affinity chromatography (FAC).
Site-specific N-linked glycosylation of receptor guanylyl cyclase C regulates ligand binding, ligand-mediated activation and interaction with vesicular integral membrane protein 36, VIP36.
Visweswariah et al., Bengaluru, India. In J Biol Chem, 2013
We also show that GC-C is the first identified receptor client of the lectin chaperone vesicular integral membrane protein, VIP36.
Subcellular localization of ERGIC-53 under endoplasmic reticulum stress condition.
Yamamoto et al., Kashiwa, Japan. In Glycobiology, 2012
ER-Golgi intermediate compartment (ERGIC)-53, VIP36 and VIPL, which have an L-type lectin domain within the luminal portion, participate in the vectorial transport of glycoproteins via sugar-protein interactions.
Molecular characterization of three L-type lectin genes from channel catfish, Ictalurus punctatus and their responses to Edwardsiella ictaluri challenge.
Liu et al., Auburn, United States. In Fish Shellfish Immunol, 2012
Three L-type lectins were cloned in the channel catfish, Ictalurus punctatus, the 53 kDa endoplasmic reticulum ER-Golgi intermediate compartment protein (ERGIC-53), the vesicular integral protein of 36 kDa (VIP36) and VIP36-like.
VIP36 protein is a target of ectodomain shedding and regulates phagocytosis in macrophage Raw 264.7 cells.
Okada et al., Tokyo, Japan. In J Biol Chem, 2012
We identified VIP36 (36-kDa vesicular integral membrane protein), a lectin domain-containing transmembrane protein postulated as a cargo receptor for Golgi-to-endoplasmic reticulum transport, as a new target for shedding and found that the shedding of VIP36 occurs mainly on the cell surface.
Role of the lectin VIP36 in post-ER quality control of human alpha1-antitrypsin.
GeneRIF
Hauri et al., Basel, Switzerland. In Traffic, 2010
Results identify the glycoprotein alpha1-antitrypsin as a cargo of VIP36.
Chemical approaches toward understanding glycan-mediated protein quality control.
Review
Ito et al., Wako, Japan. In Curr Opin Chem Biol, 2009
Involved in this process are a number of intracellular carbohydrate-recognizing proteins or carbohydrate-processing enzymes, including calnexin/calreticulin, malectin, glucosidase I (G-I) and II (G-II), UDP-glucose:glycoprotein glucosyltransferase (UGGT), cargo receptors (VIP36, ERGL, and ERGIC-53), ER 1,2-mannosidase I, ER degradation-enhancing alpha-mannosidase-like proteins (EDEMs) and ubiquitin ligase.
Role of N-glycosylation in trafficking of apical membrane proteins in epithelia.
Review
Sachs et al., Los Angeles, United States. In Am J Physiol Renal Physiol, 2009
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.
Molecular basis of sugar recognition by the human L-type lectins ERGIC-53, VIPL, and VIP36.
GeneRIF
Kato et al., Nagoya, Japan. In J Biol Chem, 2008
selective interaction of VIPL and VIP36 with the deglucosylated trimannose in the D1 branch of high-mannose-type oligosaccharides but with different pH dependence.
Stable interaction of the cargo receptor VIP36 with molecular chaperone BiP.
GeneRIF
Yamamoto et al., Chiba, Japan. In Glycobiology, 2007
VIP36 interacts with molecular chaperone BiP and has a role in the quality control of secretory proteins
Structural approaches to the study of oligosaccharides in glycoprotein quality control.
Review
Totani et al., Wako, Japan. In Curr Opin Struct Biol, 2005
These include calnexin/calreticulin, UDP-glucose:glycoprotein glucosyltransferase (UGGT), cargo receptors (such as VIP36 and ERGIC-53), mannosidase-like proteins (e.g.
Clusters of VIP-36-positive vesicles between endoplasmic reticulum and Golgi apparatus in GH3 cells.
GeneRIF
Ishikawa et al., Japan. In Cell Struct Funct, 2003
Results suggest that actin filaments are involved in glycoprotein transport between the endoplasmic reticulum and cis-Golgi cisterna by using vesicular integral membrane protein-36 (VIP36).
Lectin control of protein folding and sorting in the secretory pathway.
Review
Bergeron et al., Montréal, Canada. In Trends Biochem Sci, 2003
By contrast, sequence similarity between ERGIC-53 and vesicular integral membrane protein (VIP36), a Golgi-resident protein, leaves little doubt that a similar lectin domain is central to the transport and/or sorting functions of VIP36.
Lectins and protein traffic early in the secretory pathway.
Review
Liang et al., Basel, Switzerland. In Biochem Soc Symp, 2001
Two ERGIC-53-related proteins, VIP36 (vesicular integral membrane protein 36) and a novel ERGIC-53-like protein, ERGL, are also found in the early secretory pathway.
Quantitative ER <--> Golgi transport kinetics and protein separation upon Golgi exit revealed by vesicular integral membrane protein 36 dynamics in live cells.
GeneRIF
Stelzer et al., Heidelberg, Germany. In Mol Biol Cell, 2001
Live imaging of the canine homologous protein.
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