Spiraling in control: structures and mechanisms of the Hsp104 disaggregase
Hsp104 is a hexameric AAA+ ATPase and protein disaggregase found in yeast, which
couples ATP hydrolysis to the dissolution of diverse polypeptides trapped in toxic …
couples ATP hydrolysis to the dissolution of diverse polypeptides trapped in toxic …
Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins
By virtue of their general ability to bind (hold) translocating or unfolding polypeptides
otherwise doomed to aggregate, molecular chaperones are commonly dubbed “holdases” …
otherwise doomed to aggregate, molecular chaperones are commonly dubbed “holdases” …
Skd3 (human ClpB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations
Cells have evolved specialized protein disaggregases to reverse toxic protein aggregation
and restore protein functionality. In nonmetazoan eukaryotes, the AAA+ disaggregase …
and restore protein functionality. In nonmetazoan eukaryotes, the AAA+ disaggregase …
Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation
M Carroni, E Kummer, Y Oguchi, P Wendler, DK Clare… - Elife, 2014 - elifesciences.org
The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with
the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD) is a coiled …
the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD) is a coiled …
AAA+ proteins: one motor, multiple ways to work
Numerous ATPases associated with diverse cellular activities (AAA+) proteins form
hexameric, ring-shaped complexes that function via ATPase-coupled translocation of …
hexameric, ring-shaped complexes that function via ATPase-coupled translocation of …
Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation
Hsp104, a conserved AAA+ protein disaggregase, promotes survival during cellular stress.
Hsp104 remodels amyloids, thereby supporting prion propagation, and disassembles toxic …
Hsp104 remodels amyloids, thereby supporting prion propagation, and disassembles toxic …
Mechanistic and structural insights into the prion-disaggregase activity of Hsp104
Hsp104 is a dynamic ring translocase and hexameric AAA+ protein found in yeast, which
couples ATP hydrolysis to disassembly and reactivation of proteins trapped in soluble …
couples ATP hydrolysis to disassembly and reactivation of proteins trapped in soluble …
The Hsp104 N-terminal domain enables disaggregase plasticity and potentiation
The structural basis by which Hsp104 dissolves disordered aggregates and prions is
unknown. A single subunit within the Hsp104 hexamer can solubilize disordered …
unknown. A single subunit within the Hsp104 hexamer can solubilize disordered …
Mining disaggregase sequence space to safely counter TDP-43, FUS, and α-synuclein proteotoxicity
Hsp104 is an AAA+ protein disaggregase, which can be potentiated via diverse mutations in
its autoregulatory middle domain (MD) to mitigate toxic misfolding of TDP-43, FUS, and α …
its autoregulatory middle domain (MD) to mitigate toxic misfolding of TDP-43, FUS, and α …
Neutropenia and intellectual disability are hallmarks of biallelic and de novo CLPB deficiency
Purpose To investigate monoallelic CLPB variants. Pathogenic variants in many genes
cause congenital neutropenia. While most patients exhibit isolated hematological …
cause congenital neutropenia. While most patients exhibit isolated hematological …