The DOI matches its Crossref record; 97 of the 97 references it cites were found in a registry or an index.
The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends
Open accessAbstract
The endoplasmic reticulum (ER) represents the entry point into the secretory pathway where nascent proteins encounter a specialized environment for their folding and maturation. Inherent to these processes is a dedicated quality-control system that detects proteins that fail to mature properly and targets them for cytosolic degradation. An imbalance in protein folding and degradation can result in the accumulation of unfolded proteins in the ER, resulting in the activation of a signaling cascade that restores proper homeostasis in this organelle. The ER heat shock protein 70 (Hsp70) family member BiP is an ATP-dependent chaperone that plays a critical role in these processes. BiP interacts with specific ER-localized DnaJ family members (ERdjs), which stimulate BiP's ATP-dependent substrate interactions, with several ERdjs also binding directly to unfolded protein clients. Recent structural and biochemical studies have provided detailed insights into the allosteric regulation of client binding by BiP and have enhanced our understanding of how specific ERdjs enable BiP to perform its many functions in the ER. In this review, we discuss how BiP's functional cycle and interactions with ERdjs enable it to regulate protein homeostasis in the ER and ensure protein quality control.
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Cites
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Integrated lncRNA function upon genomic and epigenomic regulation
Herman, A. B., Tsitsipatis, D., & Gorospe, M. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.05.027 · Cited by 747
ChaperISM: improved chaperone binding prediction using position-independent scoring matrices
Gutierres, M. B. B., Bonorino, C. B. C., & Rigo, M. M. (2020) · Bioinformatics · doi:10.1093/bioinformatics/btz670 · Cited by 29
De Masi, R., & Orlando, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137373 · Cited by 20
“These molecules play a critical role not only in stimulating ATP hydrolysis of BiP, but also in regulating its various activities [350].”
BackgroundZha, J., Bi, S., Deng, M., Chen, K., Shi, P., Feng, L., He, J., Pu, X., Guo, C., Zhao, H., et al. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174107 · Cited by 18
Metadata
- Authors
- Pobre, K. F. R., Poet, G. J., & Hendershot, L. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2019-02
- Volume
- 294
- Issue
- 6
- Pages
- 2098-2108
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2904223696
- Cited by
- 429
- References
- 97
- FWCI
- 16.74
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Pobre, K. F. R., Poet, G. J., & Hendershot, L. M. (2019). The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.rev118.002804
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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