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J Biol Chem. 2016 Jan 22;291(4):1664-75. doi: 10.1074/jbc.M115.698662. Epub 2015 Nov 24.

Cold Temperature Induces the Reprogramming of Proteolytic Pathways in Yeast.

Author information

1
From the Institut de Biologia Molecular de Barcelona, Consejo Superior de Investigaciones Científicas, Barcelona Science Park, Baldiri i Reixac 15-21, 08028 Barcelona, Spain and Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115.
2
From the Institut de Biologia Molecular de Barcelona, Consejo Superior de Investigaciones Científicas, Barcelona Science Park, Baldiri i Reixac 15-21, 08028 Barcelona, Spain and.
3
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115.
4
From the Institut de Biologia Molecular de Barcelona, Consejo Superior de Investigaciones Científicas, Barcelona Science Park, Baldiri i Reixac 15-21, 08028 Barcelona, Spain and bernat.crosas@ibmb.csic.es.

Abstract

Despite much evidence of the involvement of the proteasome-ubiquitin signaling system in temperature stress response, the dynamics of the ubiquitylome during cold response has not yet been studied. Here, we have compared quantitative ubiquitylomes from a strain deficient in proteasome substrate recruitment and a reference strain during cold response. We have observed that a large group of proteins showing increased ubiquitylation in the proteasome mutant at low temperature is comprised by reverses suppressor of Ty-phenotype 5 (Rsp5)-regulated plasma membrane proteins. Analysis of internalization and degradation of plasma membrane proteins at low temperature showed that the proteasome becomes determinant for this process, whereas, at 30 °C, the proteasome is dispensable. Moreover, our observations indicate that proteasomes have increased capacity to interact with lysine 63-polyubiquitylated proteins during low temperature in vivo. These unanticipated observations indicate that, during cold response, there is a proteolytic cellular reprogramming in which the proteasome acquires a role in the endocytic-vacuolar pathway.

KEYWORDS:

Can1; Itr1; Rad23; Rpn10; endocytosis; low temperature; proteasome; protein degradation; ubiquitin; vacuole

PMID:
26601941
PMCID:
PMC4722449
DOI:
10.1074/jbc.M115.698662
[Indexed for MEDLINE]
Free PMC Article

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