Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes

Tyedmers, Jens; Lerner, Monika; Bies, Christiane; Dudek, Johanna; Skowronek, Markus H.; Haas, Ingrid G.; Heim, Nicole; Nastainczyk, Wolfgang; Volkmer, Jörg; Zimmermann, Richard

doi:10.1073/pnas.97.13.7214

Cited by 149 publications

(186 citation statements)

References 41 publications

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“…3,14,16 the Bip-Sec63 interaction was described by tyedmers et al and the effect of the r197e mutation by awad et al 17,18 So far, the latter interaction as well as the Sec62-Sec63 interaction were found to be relevant only for protein transport into the er, i.e., gating of the Sec61 complex from the closed to the open conformation; 19 in contrast, the Bip co-chaperone for gating to the closed state is still elusive. 3 See text for details.…”

Section: Resultsmentioning

confidence: 99%

Interaction ofPseudomonas aeruginosaExotoxin A with the human Sec61 complex suppresses passive calcium efflux from the endoplasmic reticulum

et al. 2013

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Section: Resultsmentioning

confidence: 99%

Interaction ofPseudomonas aeruginosaExotoxin A with the human Sec61 complex suppresses passive calcium efflux from the endoplasmic reticulum

et al. 2013

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“…These antibodies were able to immunoprecipitate native Sec61 complex from canine pancreatic microsomal extracts (Fig. 9B), albeit less efficiently as compared with Sec61␤ antibodies (25). Thus, the tyrosine 344-containing motif within loop 7 of Sec61␣ is available to antibody binding in the native Sec61 complex.…”

Section: Bip and Antibodies Directed Against The Bip Binding Site Canmentioning

confidence: 97%

“…For immunoprecipitation, canine pancreatic rough microsomes (RM) were stripped of ribosomes with puromycin and high salt, yielding puromycin and high salt treated RM (PKRM), and solubilized in 50 mM HEPES/KOH, pH 7.8, 500 mM KAc, 15% glycerol, 2.5% digitonin for 10 min on ice as described (25). Supernatant was collected after centrifugation at 16,000 ϫ g and 4°C for 10 min.…”

Section: Methodsmentioning

confidence: 99%

“…Fabs were produced from affinitypurified antibodies with the Pierce Fab Preparation Kit (Thermo Fisher Scientific) according to the manufacturer's protocol. GST-tagged ERj proteins and His-tagged BiP from hamsters were purified as described previously (25)(26)(27)(28). Fabs were analyzed by reductive or non-reductive (with or without ␤-mercaptoethanol in the sample buffer) SDS-PAGE.…”

Section: Methodsmentioning

confidence: 99%

“…Fura-2 signals were recorded and analyzed as described for naive HeLa cells. To allow the recording of D1ER and Fura-2 signals in the same cells, the filter sets were automatically exchanged in such a way that two pairs of images were obtained every 10 s. (25)(26)(27)(28). Monoclonal goat anti-GST antibodies were immobilized on a sensor chip CM5 (BIACORE).…”

Section: Methodsmentioning

confidence: 99%

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Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum

Schorr

Klein

Gamayun

et al. 2015

Journal of Biological Chemistry

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Background:The molecular chaperone immunoglobulin heavy-chain-binding protein (BiP) modulates gating of the polypeptide-conducting and calcium-permeable channel (Sec61 complex) in the membrane of the endoplasmic reticulum (ER). Results: Two co-chaperones, ERj3 and ERj6, support BiP in preventing ER calcium leakage via Sec61 complex. Conclusion: ERj3 and ERj6 facilitate Sec61 channel closing. Significance: Different co-chaperones assist BiP in Sec61 channel gating.

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hSnd2 protein represents an alternative targeting factor to the endoplasmic reticulum in human cells

et al. 2017

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Recently, understanding of protein targeting to the endoplasmic reticulum (ER) was expanded by the discovery of multiple pathways that function in parallel to the signal recognition particle (SRP). Guided entry of tail-anchored proteins and SRP independent (SND) are two such targeting pathways described in yeast. So far, no human SND component is functionally characterized. Here, we report hSnd2 as the first constituent of the human SND pathway able to support substrate-specific protein targeting to the ER. Similar to its yeast counterpart, hSnd2 is assumed to function as a membrane-bound receptor preferentially targeting precursors carrying C-terminal transmembrane domains. Our genetic and physical interaction studies show that hSnd2 is part of a complex network of targeting and translocation that is dynamically regulated.

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Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes

Cited by 149 publications

References 41 publications

Interaction ofPseudomonas aeruginosaExotoxin A with the human Sec61 complex suppresses passive calcium efflux from the endoplasmic reticulum

Interaction ofPseudomonas aeruginosaExotoxin A with the human Sec61 complex suppresses passive calcium efflux from the endoplasmic reticulum

Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum

hSnd2 protein represents an alternative targeting factor to the endoplasmic reticulum in human cells

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