Chaperone-mediated autophagy (CMA) is a selective form of autophagy in which cytosolic proteins bearing a pentapeptide motif biochemically related to the KFERQ sequence, are recognized by the heat shock protein family A member 8 (HSPA8) chaperone, delivered to the lysomal membrane, and directly translocated across the lysosomal membrane by a protein complex containing lysosomal associated membrane protein 2a (Lamp2a). Since its discovery over two decades ago, the importance of this pathway in cell proteostasis has been made increasingly apparent. Deregulation of this pathway has been implicated in a variety of diseases and conditions, including lysosomal storage diseases, cancer, neurodegeneration and even aging. Here, we describe the main molecular features of the pathway, its regulation, cross-talk with other degradation pathways and importance in disease.
Molecular control of chaperone-mediated autophagy
Jon D. Lane, Viktor I. Korolchuk, James T. Murray, Steve Catarino, Paulo Pereira, Henrique Girão; Molecular control of chaperone-mediated autophagy. Essays Biochem 12 December 2017; 61 (6): 663–674. doi: https://doi.org/10.1042/EBC20170057
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