Proteomic analysis reveals the direct recruitment of intrinsically disordered regions to stress granules in S. cerevisiae

Article Article scientifique Article Proteomic analysis reveals the direct recruitment of intrinsically disordered regions to stress granules in S. cerevisiae eng 2020-01-01 2020-01-01 author Zhu Mang 0000-0002-3177-5541 Michael Smith Laboratories, Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada author Kuechler Erich R. Michael Smith Laboratories, Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada author Zhang Joyce Michael Smith Laboratories, Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada 419441 author Matalon Or Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel author Dubreuil Benjamin Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel author Hofmann Analise Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, BC, Canada author Loewen Chris Department of Cellular and Physiological Sciences, University of British Columbia, Vancouver, BC, Canada author Levy Emmanuel Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel 417450 Département de biologie moléculaire et cellulaire (MOCEL) author Gsponer Joerg Michael Smith Laboratories, Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada author Mayor Thibault 0000-0002-9289-3939 Michael Smith Laboratories, Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, BC, Canada 89310 jcs.244657 10.1242/jcs.244657 32503941 0021-9533 https://journals.biologists.com/jcs/article/doi/10.1242/jcs.244657/266501/Proteomic-analysis-reveals-the-direct-recruitment Stress granules (SGs) are stress-induced membraneless condensates that store non-translating mRNA and stalled translation initiation complexes. While metazoan SGs are dynamic compartments where proteins can rapidly exchange with their surroundings, yeast SGs seem largely static. To gain a better understanding of the yeast SGs, we identified proteins that sediment after heat-shock by mass spectrometry. Proteins that sediment upon heat-shock are biased toward a subset of abundant proteins that are significantly enriched in intrinsically disordered regions (IDRs). Heat-induced SG localization of over 80 proteins were confirmed using microscopy, including 32 proteins not previously known to localize to SGs. We found that several IDRs were sufficient to mediate SG recruitment. Moreover, the dynamic exchange of IDRs can be observed via FRAP, while other components remain immobile. Lastly, we showed that the IDR of the Ubp3 deubiquitinase was critical for yeast SG formation. This work shows that IDRs can be sufficient for SG incorporation, can remain dynamic in vitrified SGs, and can play an important role in cellular compartmentalization upon stress. Heat shock Intrinsically disordered regions Proteomic analysis Saccharomyces cerevisiae Stress granules European Commission Infinite Protein Self-Assembly in Health and Disease 819318 Agglomerates EU H2020 true Journal of cell science f032c253-4740-4f9f-9575-d83f7617d78c Article (Published version) Restricted Article-scientifique-from-unpaywall.pdf 11221086 application/pdf bc8c8d68064474ee9cd22ee91c34875764c638afa2ce4f01328d5ebcc3b2f83f restrictedAccess

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Proteomic analysis reveals the direct recruitment of intrinsically disordered regions to stress granules in S. cerevisiae	Journal of cell science	2020	43	0
Protein kinases in control of the centrosome cycle	FEBS Letters	1999	235	0

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