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High concentration of Ca2+ (1.8 2.0 mmol/L) on the extracellular side of the plasma membrane will inhibit channel activity through binding to the luminal pore asparagines (D111, D114, and D115).
These results reveal that BiP binding to the luminal domains of Ire1 or Perk does not involve BiP's substrate binding domain.
The accumulation of unfolded proteins titrates Grp78/BiP from binding to the luminal tails of the ER transmembrane proteins PRK-like ER kinase (PERK), inositol-requiring transmembrane kinase/endonuclease (IRE-1) and activating transcription factor 6 (ATF6).
TEM investigation of the uptake revealed the presence of AuNPs in endosomes of cancer cells with most of the nanoparticles exhibiting no binding to the luminal surface of endosomes.
Early studies within the field provide evidence for the role of BiP (ER Hsp70 chaperone) in UPR activation by binding to the luminal domains and maintaining them in an inactive state (Bertolotti et al., 2000; Liu et al., 2000; Okamura et al., 2000; Ma et al., 2002; Zhou et al., 2006).
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The ER-resident chaperone immunoglobulin heavy chain-binding protein (BiP) binds to the luminal domain of the ER stress sensors and keeps them in an inactive state.
DOI: http://dx.doi.org/10.7554/eLife.03522.008 Having established that CH1 binds exclusively to BiP's substrate binding domain and that BiP's ATPase domain is responsible for its interaction with the luminal domains; we evaluated the effects of CH1 binding to the BiP-luminal domain complex using our pull down assay.
We found that binding affinities for region II IV were essentially the same as those measured for binding to the full-length luminal domain construct region I V, indicating the core interaction between UPR luminal domains and BiP maps to the luminal domain region II IV and ATPase domain, respectively.
Furthermore, protamine activated channels at low resting cytosolic Ca2+ levels (25 100 nM) even in the absence of lumenal Ca2+ or in the presence of high cytosolic Mg2+ levels, suggesting that protamine-induced RyR2 activation mainly results from electrostatic interactions and does not seem to require cytosolic or luminal Ca2+ binding to the respective activating sites.
13 Ezetimibe inhibits the intestinal absorption of luminal cholesterol by binding to the Niemann-Pick C1-like 1 sterol transporter in the membrane of the enterocyte brush border.
The ER luminal domain of Ire1 is maintained in its inactive monomeric state by binding to the ER Hsp70 chaperone Bip.
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