ArticleBiomolecules2015
Sulfatide-Hsp70 interaction promotes Hsp70 clustering and stabilizes binding to unfolded protein.
Article in Biomolecules, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 11 citations in OpenAlex.
- Conformational dynamics of free and membrane-bound human Hsp70 in model cytosolic and endo-lysosomal environments.Communications biology · 2021Article
- Characterization of the Relationship between the Chaperone and Lipid-Binding Functions of the 70-kDa Heat-Shock Protein, HspA1A.International journal of molecular sciences · 2020Article
- Verotoxin Receptor-Based Pathology and Therapies.Frontiers in cellular and infection microbiology · 2020Review
- Properties, metabolism and roles of sulfogalactosylglycerolipid in male reproduction.Progress in lipid research · 2018Review
- Biochemical characterization of the interaction between HspA1A and phospholipids.Cell stress & chaperones · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 70-kDa heat shock protein (Hsp70), one of the major stress-inducible molecular chaperones, is localized not only in the cytosol, but also in extracellular milieu in mammals. Hsp70 interacts with various cell surface glycolipids including sulfatide (3'-sulfogalactosphingolipid). However, the molecular mechanism, as well as the biological relevance, underlying the glycolipid-Hsp70 interaction is unknown. Here we report that sulfatide promotes Hsp70 oligomerization through the N-terminal ATPase domain, which stabilizes the binding of Hsp70 to unfolded protein in vitro. We find that the Hsp70 oligomer has apparent molecular masses ranging from 440 kDa to greater than 669 kDa. The C-terminal peptide-binding domain is dispensable for the sulfatide-induced oligomer formation. The oligomer formation is impaired in the presence of ATP, while the Hsp70 oligomer, once formed, is unable to bind to ATP. These results suggest that sulfatide locks Hsp70 in a high-affinity state to unfolded proteins by clustering the peptide-binding domain and blocking the binding to ATP that induces the dissociation of Hsp70 from protein substrates.
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Registered trials
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