Subcellular localization of the J-protein Sis1 regulates the heat shock response.
Cell Nucleolus
/ metabolism
Cell Nucleus
/ metabolism
Cytosol
/ metabolism
DNA-Binding Proteins
/ metabolism
Endoplasmic Reticulum
/ metabolism
Gene Expression Regulation, Fungal
HSP40 Heat-Shock Proteins
/ metabolism
HSP70 Heat-Shock Proteins
/ metabolism
Heat-Shock Proteins
/ metabolism
Heat-Shock Response
Models, Biological
Molecular Chaperones
/ metabolism
Mutation
/ genetics
Proteasome Endopeptidase Complex
/ metabolism
Protein Binding
Protein Transport
Proteostasis
Saccharomyces cerevisiae
/ genetics
Saccharomyces cerevisiae Proteins
/ metabolism
Subcellular Fractions
/ metabolism
Transcription Factors
/ metabolism
Transcriptome
/ genetics
Journal
The Journal of cell biology
ISSN: 1540-8140
Titre abrégé: J Cell Biol
Pays: United States
ID NLM: 0375356
Informations de publication
Date de publication:
04 01 2021
04 01 2021
Historique:
received:
22
05
2020
revised:
13
10
2020
accepted:
06
11
2020
entrez:
16
12
2020
pubmed:
17
12
2020
medline:
19
5
2021
Statut:
ppublish
Résumé
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 the nucleoplasm, where it promotes Hsp70 binding to the transcription factor Hsf1, repressing the HSR. Upon heat shock, Sis1 forms an interconnected network with other proteostasis factors that spans the nucleolus and the surface of the endoplasmic reticulum. We propose that localization of Sis1 to this network directs Hsp70 activity away from Hsf1 in the nucleoplasm, leaving Hsf1 free to induce the HSR. In this manner, Sis1 couples HSR activation to the spatial organization of the proteostasis network.
Identifiants
pubmed: 33326013
pii: 211600
doi: 10.1083/jcb.202005165
pmc: PMC7748816
pii:
doi:
Substances chimiques
DNA-Binding Proteins
0
HSF1 protein, S cerevisiae
0
HSP40 Heat-Shock Proteins
0
HSP70 Heat-Shock Proteins
0
Heat-Shock Proteins
0
Molecular Chaperones
0
SIS1 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
Transcription Factors
0
Proteasome Endopeptidase Complex
EC 3.4.25.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIH HHS
ID : DP5 OD017941
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM124446
Pays : United States
Commentaires et corrections
Type : CommentIn
Informations de copyright
© 2020 Feder et al.
Références
Nat Rev Neurosci. 2003 Jan;4(1):49-60
pubmed: 12511861
Cold Spring Harb Perspect Biol. 2020 Jan 2;12(1):
pubmed: 30833457
J Cell Biol. 1988 Jul;107(1):17-31
pubmed: 3292539
Cell Rep. 2014 Nov 6;9(3):955-66
pubmed: 25437552
Cell. 2007 Sep 21;130(6):1005-18
pubmed: 17889646
Mol Biol Cell. 2018 Dec 15;29(26):3168-3182
pubmed: 30332327
Nat Rev Mol Cell Biol. 2018 Jan;19(1):4-19
pubmed: 28852220
Proc Natl Acad Sci U S A. 1998 Dec 22;95(26):15253-8
pubmed: 9860955
Bio Protoc. 2017 Jun 20;7(12):
pubmed: 29104895
Genes Dev. 1998 Mar 1;12(5):654-66
pubmed: 9499401
Elife. 2018 Feb 02;7:
pubmed: 29393852
Cell. 2014 Oct 23;159(3):530-42
pubmed: 25417105
EMBO J. 2020 Jul 15;39(14):e104096
pubmed: 32490574
Cell. 2012 Nov 21;151(5):1042-54
pubmed: 23178123
Nat Commun. 2019 Oct 24;10(1):4851
pubmed: 31649258
Nature. 1999 Apr 29;398(6730):818-23
pubmed: 10235265
Adv Exp Med Biol. 2020;1243:41-50
pubmed: 32297210
Mol Cell. 2008 Sep 26;31(6):925-32
pubmed: 18922474
Science. 2014 Oct 24;346(6208):1257998
pubmed: 25342811
Mol Cell. 2016 Jul 7;63(1):60-71
pubmed: 27320198
J Cell Biol. 2017 May 1;216(5):1231-1241
pubmed: 28400444
Am J Physiol Cell Physiol. 2017 Feb 1;312(2):C93-C102
pubmed: 27856431
Elife. 2016 Nov 10;5:
pubmed: 27831465
Annu Rev Biochem. 2015;84:435-64
pubmed: 25784053
Annu Rev Biochem. 2011;80:1089-115
pubmed: 21417720
Annu Rev Biochem. 2013;82:323-55
pubmed: 23746257
Cell Syst. 2018 Feb 28;6(2):192-205.e3
pubmed: 29361465
Nat Rev Mol Cell Biol. 2019 Jul;20(7):421-435
pubmed: 30733602
Nature. 2008 Aug 28;454(7208):1088-95
pubmed: 18756251
Elife. 2019 Mar 07;8:
pubmed: 30843788
Cell. 1998 Aug 21;94(4):471-80
pubmed: 9727490
Trends Biochem Sci. 2017 May;42(5):355-368
pubmed: 28314505
Cell. 2013 Jul 3;154(1):134-45
pubmed: 23791384
Cell Rep. 2018 Mar 20;22(12):3099-3106
pubmed: 29562166
J Biol Chem. 2004 Aug 20;279(34):35692-701
pubmed: 15178690
Nat Methods. 2015 Jun;12(6):480-1
pubmed: 26020498
Mol Cell. 2018 Jan 18;69(2):227-237.e4
pubmed: 29290615
Expert Opin Ther Targets. 2009 Apr;13(4):469-78
pubmed: 19335068
Trends Cell Biol. 2016 Jan;26(1):17-28
pubmed: 26597576
Exp Cell Res. 2020 Nov 1;396(1):112246
pubmed: 32861670
Nat Struct Biol. 1997 May;4(5):342-9
pubmed: 9145101
J Cell Sci. 1992 Nov;103 ( Pt 3):857-62
pubmed: 1478975
Cell Rep. 2019 Jan 2;26(1):18-28.e5
pubmed: 30605674
Annu Rev Biochem. 2017 Jun 20;86:193-224
pubmed: 28460188
Elife. 2019 May 24;8:
pubmed: 31124783
J Biol Chem. 2013 Apr 26;288(17):12197-213
pubmed: 23447536
Cell. 2015 Sep 10;162(6):1286-98
pubmed: 26359986
Nat Cell Biol. 2013 Oct;15(10):1231-43
pubmed: 24036477
Nat Rev Drug Discov. 2011 Dec 01;10(12):930-44
pubmed: 22129991
IUBMB Life. 1999 Oct;48(4):429-33
pubmed: 10632574
Elife. 2019 Sep 25;8:
pubmed: 31552827
Cell. 2008 Jan 11;132(1):101-12
pubmed: 18191224
Genetics. 2013 Nov;195(3):643-81
pubmed: 24190922
J Biol Chem. 2019 Aug 9;294(32):12191-12202
pubmed: 31239354
Science. 2019 Jul 26;365(6451):342-347
pubmed: 31296649
EMBO J. 2015 Mar 12;34(6):778-97
pubmed: 25672362