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TitleConformational plasticity of a BiP-GRP94 chaperone complex.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 10, Page 1947-1958, Year 2025
Publish dateJul 14, 2025
AuthorsJoel Cyrille Brenner / Linda Charlotte Zirden / Lana Buzuk / Yasser Almeida-Hernandez / Lea Radzuweit / Joao Diamantino / Farnusch Kaschani / Markus Kaiser / Elsa Sanchez-Garcia / Simon Poepsel / Doris Hellerschmied /
PubMed AbstractHsp70 and Hsp90 chaperones and their regulatory cochaperones are critical for maintaining protein homeostasis. Glucose-regulated protein 94 (GRP94), the sole Hsp90 chaperone in the secretory pathway ...Hsp70 and Hsp90 chaperones and their regulatory cochaperones are critical for maintaining protein homeostasis. Glucose-regulated protein 94 (GRP94), the sole Hsp90 chaperone in the secretory pathway of mammalian cells, is essential for the maturation of important secretory and transmembrane proteins. Without the requirement of cochaperones, the Hsp70 protein BiP controls regulatory conformational changes of GRP94, the structural basis of which has remained elusive. Here we biochemically and structurally characterize the formation of a BiP-GRP94 chaperone complex and its transition to a conformation expected to support the loading of substrate proteins from BiP onto GRP94. BiP initially binds to the open GRP94 dimer through an interaction interface that is conserved among Hsp70 and Hsp90 paralogs. Subsequently, binding of a second BiP protein stabilizes a semiclosed GRP94 dimer, thereby advancing the chaperone cycle. Our findings highlight a fundamental mechanism of direct Hsp70-Hsp90 cooperation, independent of cochaperones.
External linksNat Struct Mol Biol / PubMed:40659993 / PubMed Central
MethodsEM (single particle)
Resolution14.0 - 15.0 Å
Structure data

EMDB-19600: GRP94-BiP complex, pre-loading conformation
Method: EM (single particle) / Resolution: 15.0 Å

EMDB-19601: GRP94-BiP complex, loading conformation
Method: EM (single particle) / Resolution: 14.0 Å

Source
  • Homo sapiens (human)
  • Rhodococcus (bacteria)

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