Proteomics

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Subcellular localization of the J-protein Sis1 regulates the heat shock response

ABSTRACT: How heat shock inducesthe heat shock response (HSR) – a gene expression program encoding chaperones and other protein homeostasis (proteostasis) factors –remains an unresolved question in eukaryotic cell biology. Here we show that subcellular localization of the conserved J-protein Sis1 is a key regulator of the HSRin yeast. Under nonstress conditions, nucleoplasmic Sis1 promotes interaction between the chaperone Hsp70 and the transcription factor Hsf1to repress the HSR. Heat shock triggers Sis1 to localize to the nucleolar periphery and condense on the ER surface with the ribosome quality control complex. Sis1 recruits the proteasome to this spatial network.Through localization dynamics, Sis1 relaysthe condition of the proteome to Hsf1.Thus, the activation state of the HSR is built into spatial organization of the proteostasis network.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Donald Wolfgeher  

LAB HEAD: David Pincus

PROVIDER: PXD019170 | Pride | 2021-03-24

REPOSITORIES: Pride

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Subcellular localization of the J-protein Sis1 regulates the heat shock response.

Feder Zoë A ZA   Ali Asif A   Singh Abhyudai A   Krakowiak Joanna J   Zheng Xu X   Bindokas Vytas P VP   Wolfgeher Donald D   Kron Stephen J SJ   Pincus David D  

The Journal of cell biology 20210101 1

Cells exposed to heat shock induce a conserved gene expression program, the heat shock response (HSR), encoding protein homeostasis (proteostasis) factors. Heat shock also triggers proteostasis factors to form subcellular quality control bodies, but the relationship between these spatial structures and the HSR is unclear. Here we show that localization of the J-protein Sis1, a cofactor for the chaperone Hsp70, controls HSR activation in yeast. Under nonstress conditions, Sis1 is concentrated in  ...[more]

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