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Serena Carra, M.Sc., Ph.D. - "The HSPB8-BAG3-HSP70 chaperone complex: implication in protein homeostasis and neurodegenerative diseases"

University of Modena and Reggio Emilia, Modena, Italy
When Dec 12, 2017
from 12:00 PM to 01:30 PM
Where Tigem Auditorium "Vesuvius"
Contact Name
Contact Phone 081-19230659
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Abstract
HSPB8 is a member of the mammalian small Heat Shock Protein family (HSPB1-HSPB10) that is ubiquitously expressed. Unlike HSPB1, HSPB4 and HSPB5, which mainly form homo- and hetero-oligomers of variable size by associating with themselves or with other HSPBs, HSPB8 forms a stable and stoichiometric complex with HSPA8/HSPA1A and its co-chaperone BAG3. Binding to BAG3 regulates HSPB8 stability, function and subcellular localization. Here, I will summarize key findings that demonstrate the role of the HSPB8-BAG3-HSPA1A chaperone complex in buffering misfolded proteins, including defective ribosomal products, and targeting them to the macroautophagy machinery for clearance. The concerted action of these three partners allows to efficiently bind to and hold misfolded species (HSPB8) and to transfer them to the autophagic vacuoles (HSPA1A and BAG3), via subsequent association with the autophagic receptor p62/SQSTM1 and the motor protein dynein. I will discuss the implication of the HSPB8-BAG3-HSPA1A chaperone complex in the maintenance of protein homeostasis under pathological conditions characterized by the accumulation of aggregation-prone proteins. I will report the identification of a novel role of the HSPB8-BAG3-HSPA1A chaperone complex in the maintenance of stress granule composition and dynamics and I will discuss how its deregulation may contribute to neurodegenerative disease progression. Finally, I will discuss how deregulation of the HSPB8-BAG3-HSPA1A complex, due to mutations in HSPB8, causes motor neuropathy and muscle atrophy

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