Eukaryotic cells use autophagy and the ubiquitin–proteasome system as their major protein degradation pathways. Upon proteasomal impairment, cells switch to autophagy to ensure proper clearance of clients (the proteasome-to-autophagy switch). How the proteasomal clients are re-routed to the autophagosomal pathway has remained unclear. We found that several stress pathways that are induced upon disturbances in protein homeostasis as well as by direct chemically-induced proteasomal inhibition increase the protein levels of BAG3, a partner of the heat shock proteins HSPB8 and Hsp70. BAG3 induces the sequestration of Hsp70-bound proteasomal clients into cytoplasmic puncta which leads to their re-routing to autophagosomes for degradation. This occurs through competitive inhibition with its family member BAG1, which normally directs Hsp70-bound clients to the proteasome.
|Data di pubblicazione:||2013|
|Titolo:||BAG3-mediated re-routing of protein degradation towards autophagy upon proteasomal impairment|
|Autore/i:||Minoia, Melania; Boncoraglio, Alessandra; Vinet, Jonathan; Brunsting, Jeanette F.; Poletti, Angelo; Krom, Sabine; Reits, Eric; Kampinga, Harm H.; Carra, Serena|
|Nome del convegno:||The biology of molecular chaperones: From molecules, organelles and cells to misfolding diseases.|
|Data del convegno:||17-22 Maggio 2013|
|Luogo del convegno:||Santa Margherita di Pula, Italy|
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