KAR2 Antibody

1. Reductive stress in the endoplasmic reticulum (ER) inhibits the Ost3-dependent N-glycosylation of Sil1, which regulates specific BiP functions appropriate to the needs of the ER under reductive stress. PMID: 29109265
2. Here the authors demonstrate that BiP's nucleotide exchange factor - Sil1 - can reverse BiP cysteine oxidation. PMID: 28257000
3. The authors found that the ATPase activity displayed by unmodified Kar2 is fully maintained when Cys63 is replaced with Ala or Val. PMID: 27543005
4. the susceptibility of BiP to modification with glutathione may serve also to prevent irreversible oxidation of BiP by peroxide. PMID: 26865632
5. Alteration of KAR2 (BiP) activity upon oxidation helps cells cope with disruption to oxidative folding within the endoplasmic reticulum during oxidative stress. PMID: 25053742
6. Data indicate that BiP (GRP78/Kar2) stabilizes torsinA and torsinADeltaE in mammalian cells. PMID: 24627482
7. The inability to induce KAR2 under stress had no effect on its known housekeeping functions. PMID: 22190740
8. Kar2p mobility represents a powerful new tool capable of distinguishing between the different mechanisms leading to unfolded protein response activation in living cells. PMID: 22219379
9. Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor PMID: 21675960
10. A major BiP cochaperone in antibody folding, ERdj3, modulated the conformational space of BiP in a nucleotide-dependent manner, placing the lid subdomain in an open, protein-accepting state. PMID: 21217698
11. Interactions between Kar2p and its nucleotide exchange factors Sil1p and Lhs1p are mechanistically distinct PMID: 20430899
12. in the ER stress-sensory system BiP is not the principal determinant of Ire1 activity, but an adjustor for sensitivity to various stresses PMID: 15520230
13. The introduction of Kar2p improves secretory proteins in Pichia pastoris secretion 4-7 times. PMID: 16889384
14. glutamine 88 is part of or close to the Ire1p-binding site displayed on the ATP-bound conformation of Kar2p PMID: 17276461
15. Study identified 87 Kar2p-secreting strains, including a number of known components in secretory protein modification and sorting. PMID: 19433630

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KEGG: sce:YJL034W

STRING: 4932.YJL034W