Yeast GTB1 encodes a subunit of glucosidase II required for glycoprotein processing in the endoplasmic reticulum (Q27933980)

Glucan 1,3-alpha-glucosidase ROT2 YBR229C

GOA release 2020-03-11

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Journal of Biological Chemistry

GOA release 2020-03-11

author name string

Barrie M Wilkinson

series ordinal

1

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Jessica Purswani

series ordinal

2

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Colin J Stirling

series ordinal

3

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language of work or name

English

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publication date

10 March 2006

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published in

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1 December 2016

281

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issue

10

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page(s)

6325-33

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cites work

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Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase

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Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins

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Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit

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Genetic evidence for the heterodimeric structure of glucosidase II. The effect of disrupting the subunit-encoding genes on glycoprotein folding

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The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo

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The alpha- and beta-subunits are required for expression of catalytic activity in the hetero-dimeric glucosidase II complex from human liver

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More than one glycan is needed for ER glucosidase II to allow entry of glycoproteins into the calnexin/calreticulin cycle

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Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease

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Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease

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Molecular characterization of hepatocystin, the protein that is defective in autosomal dominant polycystic liver disease.

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Abnormal hepatocystin caused by truncating PRKCSH mutations leads to autosomal dominant polycystic liver disease

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Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure

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LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum

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Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo

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Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p

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Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex

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Two distinct domains of the beta-subunit of glucosidase II interact with the catalytic alpha-subunit

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The MRH domain suggests a shared ancestry for the mannose 6-phosphate receptors and other N-glycan-recognising proteins

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New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus

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KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene

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Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation

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Yeast mutants deficient in protein glycosylation

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ERAD: the long road to destruction

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Effect of bromoconduritol on glucosidase II from rat liver. A new kinetic model for the binding and hydrolysis of the substrate

21 January 2018

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Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus.

21 January 2018

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P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue

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Uridine diphosphate-glucose transport into the endoplasmic reticulum of Saccharomyces cerevisiae: in vivo and in vitro evidence

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Identifiers

DOI

10.1074/JBC.M510455200

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Consolidated OpenCitations Corpus – April 2017

3621862

3621862

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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