PMID:19363271

Citation	Tortosa, E, Santa-Maria, I, Moreno, F, Lim, F, Perez, M and Avila, J (2009) Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein. J. Alzheimers Dis. 17:319-25
Abstract	Tau pathology, associated with Alzheimer's disease, is characterized by the presence of phosphorylated and aggregated tau. Phosphorylation of tau takes place mainly in the vicinity of the tubulin-binding region of the molecule and its self aggregation is also mediated via this tubulin-binding region. Tau phosphorylation and aggregation have been related with conformational changes of the protein. These changes could be regulated by chaperones such as heat shock proteins, since one of these, heat shock protein 90 (Hsp90), has already been described as a putative tau-binding protein. In this work, we have confirmed the interaction of Hsp90 with tau protein and report that binding of Hsp90 to tau facilitates a conformational change that could result in its phosphorylation by glycogen synthase kinase 3 and its aggregation into filamentous structures.
Links	PubMed Online version:10.3233/JAD-2009-1049
Keywords	Animals; Biophysical Phenomena/physiology; Brain/metabolism; Glycogen Synthase Kinase 3/metabolism; Glycogen Synthase Kinase 3 beta; HSP90 Heat-Shock Proteins/metabolism; HSP90 Heat-Shock Proteins/ultrastructure; Humans; Immunoblotting/methods; Immunoprecipitation/methods; Microscopy, Electron, Scanning/methods; Phosphorylation; Protein Binding/drug effects; Protein Binding/physiology; Protein Conformation; Rats; tau Proteins/metabolism; tau Proteins/ultrastructure
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
HUMAN:HS90A	involved_in	GO:0032273: positive regulation of protein polymerization	ECO:0000314: direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P10636)	Seeded From UniProt	complete
HUMAN:HS90A	enables	GO:0048156: tau protein binding	ECO:0000353: physical interaction evidence used in manual assertion	UniProtKB:P19332	F	occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
HUMAN:HS90A	involved_in	GO:0001934: positive regulation of protein phosphorylation	ECO:0000314: direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P10636)	Seeded From UniProt	complete
HUMAN:HS90A	involved_in	GO:1902949: positive regulation of tau-protein kinase activity	ECO:0000314: direct assay evidence used in manual assertion		P	has_input:(UniProtKB:P49841)	Seeded From UniProt	complete
RAT:TAU	enables	GO:0051879: Hsp90 protein binding	ECO:0000353: physical interaction evidence used in manual assertion	UniProtKB:P07900	F	occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
RAT:HS90A	enables	GO:0048156: tau protein binding	ECO:0000353: physical interaction evidence used in manual assertion	RGD:69329	F		Seeded From UniProt	complete
RAT:TAU	enables	GO:0051879: Hsp90 protein binding	ECO:0000353: physical interaction evidence used in manual assertion	UniProtKB:P07900	F	occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
RAT:TAU	enables	GO:0051879: Hsp90 protein binding	ECO:0000353: physical interaction evidence used in manual assertion	RGD:631409	F		Seeded From UniProt	complete
HUMAN:HS90A	enables	GO:0048156: tau protein binding	ECO:0000353: physical interaction evidence used in manual assertion	UniProtKB:P19332	F	occurs_in:(UBERON:0000955)	Seeded From UniProt	complete
HUMAN:HS90A	involved_in	GO:1902949: positive regulation of tau-protein kinase activity	ECO:0000314: direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P49841)	Seeded From UniProt	complete
HUMAN:HS90A	involved_in	GO:0001934: positive regulation of protein phosphorylation	ECO:0000314: direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P10636)	Seeded From UniProt	complete
HUMAN:HS90A	involved_in	GO:0032273: positive regulation of protein polymerization	ECO:0000314: direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P10636)	Seeded From UniProt	complete

References

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