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Not quite the SSAme: unique roles for the yeast cytosolic Hsp70s

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Abstract

The Heat Shock Protein 70s (Hsp70s) are an essential family of proteins involved in folding of new proteins and triaging of damaged proteins for proteasomal-mediated degradation. They are highly conserved in all organisms, with each organism possessing multiple highly similar Hsp70 variants (isoforms). These isoforms have been previously thought to be identical in function differing only in their spatio-temporal expression pattern. The model organism Saccharomyces cerevisiae (baker’s yeast) expresses four Hsp70 isoforms Ssa1, 2, 3 and 4. Here, we review recent findings that suggest that despite their similarity, Ssa isoforms may have unique cellular functions.

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Acknowledgements

This work was supported by NCI R15CA208773 (AWT).

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Author notes

  1. Sarah K. Lotz and Laura E. Knighton made equal contributions to this study.

Authors and Affiliations

  1. Department of Biological Sciences, The University of North Carolina At Charlotte, Charlotte, NC, 28223, USA

    Sarah K. Lotz, Laura E. Knighton,  Nitika & Andrew W. Truman

  2. Centre for Biomedical Science Research, School of Clinical and Applied Sciences, Leeds Beckett University, Leeds, UK

    Gary W. Jones

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  1. Sarah K. Lotz
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  2. Laura E. Knighton
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  3. Nitika
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  4. Gary W. Jones
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Correspondence to Andrew W. Truman.

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Communicated by M. Kupiec.

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Lotz, S.K., Knighton, L.E., Nitika et al. Not quite the SSAme: unique roles for the yeast cytosolic Hsp70s. Curr Genet 65, 1127–1134 (2019). https://doi.org/10.1007/s00294-019-00978-8

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