The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane.

ABSTRACT: Chaperone-mediated autophagy (CMA) is a selective type of autophagy by which specific cytosolic proteins are sent to lysosomes for degradation. Substrate proteins bind to the lysosomal membrane through the lysosome-associated membrane protein type 2A (LAMP-2A), one of the three splice variants of the lamp2 gene, and this binding is limiting for their degradation via CMA. However, the mechanisms of substrate binding and uptake remain unknown. We report here that LAMP-2A organizes at the lysosomal membrane into protein complexes of different sizes. The assembly and disassembly of these complexes are a very dynamic process directly related to CMA activity. Substrate proteins only bind to monomeric LAMP-2A, while the efficient translocation of substrates requires the formation of a particular

SUBMITTER: Bandyopadhyay U 

PROVIDER: S-EPMC2546938 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature