Structural transitions modulate the chaperone activities of Grp94

A recent study by Amankwah et al. reports how co-chaperone proteins and ATP hydrolysis fine-tune the function of endoplasmic reticulum (ER)-resident Hsp90 paralog Grp94. A recent study by Amankwah et al. reports how co-chaperone proteins and ATP hydrolysis fine-tune the function of endoplasmic retic...

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Veröffentlicht in:	Trends in biochemical sciences (Amsterdam. Regular ed.) 2024-09, Vol.49 (9), p.752-753
Hauptverfasser:	Mirikar, Duhita, Bushman, Yevheniia, Truman, Andrew W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphate - metabolism Animals BiP DEER endoplasmic reticulum (ER) Endoplasmic Reticulum - metabolism Grp94 Hsp90 Humans Membrane Glycoproteins - chemistry Membrane Glycoproteins - metabolism Molecular Chaperones - chemistry Molecular Chaperones - metabolism protein folding
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Zusammenfassung:	A recent study by Amankwah et al. reports how co-chaperone proteins and ATP hydrolysis fine-tune the function of endoplasmic reticulum (ER)-resident Hsp90 paralog Grp94. A recent study by Amankwah et al. reports how co-chaperone proteins and ATP hydrolysis fine-tune the function of endoplasmic reticulum (ER)-resident Hsp90 paralog Grp94.
ISSN:	0968-0004
DOI:	10.1016/j.tibs.2024.06.007