Chaperone-mediated autophagy: Key mechanisms and its role in protein turnover

Chaperone-mediated autophagy (CMA) is a highly selective cellular degradation pathway responsible for the turnover of specific cytosolic proteins. This process relies on the recognition of protein substrates containing KFERQ-like motifs by the chaperone protein Hsc70, facilitating their translocation into lysosomes via LAMP-2A. CMA plays a pivotal role in maintaining protein homeostasis, particularly during cellular stress, and contributes to the removal of damaged or misfolded proteins. Dysregulation of CMA has been linked to various diseases, including neurodegenerative disorders and cancer. Understanding the intricate molecular mechanisms of CMA and its regulatory pathways is essential for developing potential therapeutic strategies. This work highlights the key aspects of CMA, the method to study chaperon-mediated autophagy, and its significance in protein turnover, emphasizing the importance of research into this process to address a range of human diseases.