BiP chaperones ER entry

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BiP chaperones ER entry

gate that guards the translocon is opened and closed by ATP cycles that also give the same protein chaperone activity, as shown on page 389 by Alder et al. The translocon is an aqueous pore in the ER membrane through which secreted proteins pass during translation. To prevent the unwanted passage of ions, unused pores are plugged on the lumen side by the action of BiP. Within the ER, BiP is als...

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BiP Co-chaperones and ER Calcium Leakage

Stefan Schorr, Marie-Christine Klein, Igor Gamayun, Armin Melnyk, Martin Jung, Nico Schäuble, Qian Wang, Birgit Hemmis, Florian Bochen, Markus Greiner, Pavel Lampel, Sabine Katharina Urban, Sarah Haßdenteufel, Johanna Dudek, Xing-Zhen Chen, Richard Wagner, Adolfo Cavalié, and Richard Zimmermann Medical Biochemistry and Molecular Biology, Saarland University, 66421 Homburg, Germany; Department o...

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Generation of human ER chaperone BiP in yeast Saccharomyces cerevisiae

BACKGROUND Human BiP is traditionally regarded as a major endoplasmic reticulum (ER) chaperone performing a number of well-described functions in the ER. In recent years it was well established that this molecule can also be located in other cell organelles and compartments, on the cell surface or be secreted. Also novel functions were assigned to this protein. Importantly, BiP protein appears ...

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p42: luteolin counteracts er stress in pc12 cells through moderating er chaperones and heat shock proteins

luteolin, as a natural polyphenolic compound, has neuroprotective effect and exerts its function by attenuation of apoptosis and oxidative stress factors. emerging evidences indicate that oxidative stress leads to neurodegeneration but is not the initial event and endoplasmic reticulum stress (er) is often considered to be the stimulus event which is caused by accumulating of misfolded proteins...

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 2005

ISSN: 1540-8140,0021-9525

DOI: 10.1083/jcb1683iti2