Combining results from the current research, we summarize the basic processes, regulatory mechanisms, and physiological functions of CMA and discuss its critical role in the development of diseases.īasic process Chaperone-mediated autophagy (CMA) Microautophagy Physiological function Regulation. It has been reported that peroxide accumulation, aging and/or other pathological signals interfere with CMA function, which in turn induces neurodegenerative diseases, cancer, and other diseases. However, very little is known about how IGF-IR protein levels are degraded by HSP90 inhibitors in pancreatic cancer (PC). In the past few years, we have acquired a better understanding of how CMA is regulated. 1 Altmetric Metrics Abstract Enhancement of insulin-like growth factor 1 receptor (IGF-IR) degradation by heat shock protein 90 (HSP90) inhibitor is a potential antitumor therapeutic strategy. By degrading specific target proteins in a timely manner, CMA is involved in a variety of cellular activities. This process involves the recognition of the substrate, the unfolding and translocation of the substrate, and the degradation of the substrate. Chaperone-mediated autophagy (CMA) was the first lysosomal process to be discovered by which intracellular components are selectively degraded. Thus, autophagy flux may indeed be increasingly and potentially systemically controlled in aged patients to better understand the development of autophagy deregulation and how it contributes to disease. Protein synthesis and degradation coordinately regulate protein homeostasis. CMA, chaperone-mediated autophagy HSC70, heat shock chaperone 70 LAMP2. Protein homeostasis is essential for maintaining cell survival.

Chaperone mediated autophagy 2019