Abstract
The Hsp70/Hsp90 organising protein (Hop, also known as stress-inducible protein 1/STI1/STIP1) has received considerable attention for diverse cellular functions in both healthy and diseased states. There is extensive evidence that intracellular Hop is a co-chaperone of the major chaperones Hsp70 and Hsp90, playing an important role in the productive folding of Hsp90 client proteins, although recent evidence suggests that eukaryotic Hop is regulatory within chaperone complexes rather than essential. Consequently, Hop is implicated in many key signalling pathways, including aberrant pathways leading to cancer. Hop is also secreted, and it is now well established that Hop interacts with the prion protein, PrPC, to mediate multiple signalling events. The intracellular and extracellular forms of Hop most likely represent two different isoforms, although the molecular determinants of these divergent functions are yet to be identified. There is also a growing body of research that reports the involvement of Hop in cellular activities that appear independent of either chaperones or PrPC. While the various cellular functions of Hop have been described, its biological function remains elusive. However, recent knockout studies in mammals suggest that Hop has an important role in embryonic development. This review provides a critical overview of the latest molecular, cellular and biological research on Hop, critically evaluating its function in healthy systems and how this function is adapted in diseased states.
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Acknowledgements
KS is supported by a DAAD-National Research Foundation (NRF, South Africa) PhD fellowship and Rhodes University. GLB is supported by the NRF (Grant No. 114822), Rhodes University and The University of Notre Dame Australia. ALE is supported by a Newton Advanced Fellowships from the Academy of Medical Sciences (UK) and grants from the Resilient Futures Challenge-Led Initiative from the Royal Society (UK) (Grant No. CHL\R1\180142), the South African Research Chairs Initiative of the Department of Science and Technology (DST) and the NRF (Grant No. 98566), Poliomyelitis Research Foundation (PRF, South Africa) (Grant No. 18/06), GlaxoSmithKline (GSK)/Tres Cantos Open Lab Foundation (TCOLF) grant (TC290), South African Medical Research Council Self-Initiated Research Grant, Rhodes University and the Grand Challenges Africa Drug Discovery Programme (which is a partnership between the African Academy of Sciences [AAS], the Bill & Melinda Gates Foundation, Medicines for Malaria Venture [MMV] and the University of Cape Town Drug Discovery and Development Centre [H3D]) (Grant No. GCA/DD/rnd3/043). The views reflected in this document are those of the authors and should in no way be attributed to the Academy of Medical Sciences, Royal Society, NRF, PRF, SA-MRC, GSK/TCOLF, Rhodes University or AAS.
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Schwarz, K., Baindur-Hudson, S., Blatch, G.L., Edkins, A.L. (2023). Hsp70/Hsp90 Organising Protein (Hop): Coordinating Much More than Chaperones. In: Edkins, A.L., Blatch, G.L. (eds) The Networking of Chaperones by Co-Chaperones. Subcellular Biochemistry, vol 101. Springer, Cham. https://doi.org/10.1007/978-3-031-14740-1_3
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