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HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum
Jie Wang1, Jessica Lee1, David Liem1
1Departments of Physiology, Medicine (Cardiology) and Bioinformatics, NIH BD2K Center of Excellence for Biomedical Computing, University of California Los Angeles, Los Angeles, CA 90095, USA.
Gene
|March 14, 2017
Summary
The binding immunoglobulin protein (BiP) is a crucial chaperone in the endoplasmic reticulum, aiding protein folding and cellular stress responses. Its dysregulation is linked to various diseases, making it a therapeutic target.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- The binding immunoglobulin protein (BiP) is a conserved Hsp70 chaperone in the endoplasmic reticulum (ER) lumen.
- BiP plays vital roles in protein folding, translocation, calcium homeostasis, and ER-associated degradation (ERAD).
Purpose of the Study:
- To elucidate the multifaceted functions of BiP in cellular processes.
- To highlight the role of BiP in disease pathogenesis and its potential as a therapeutic target.
Main Methods:
- Review of existing literature on BiP's structure and function.
- Analysis of BiP's involvement in cellular stress responses like the unfolded protein response (UPR).
Main Results:
- BiP regulates protein folding, ER import, Ca2+ homeostasis, and ERAD.
- BiP modulates UPR, autophagy, and apoptosis pathways in response to cellular stress.
- Post-translational modifications (PTMs) of BiP influence its activity and cellular availability.
Conclusions:
- BiP is a master regulator of ER function with critical roles in cell survival and homeostasis.
- BiP's association with cancer, cardiovascular, neurodegenerative, and immunological diseases underscores its clinical significance.
- Targeting BiP presents a promising therapeutic strategy for various diseases, particularly cancer.
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