A novel mechanism for the retention of Golgi membrane proteins mediated by the Bre5p/Ubp3p deubiquitinase complex.

Molecular Biology of the Cell
Peng WangDavid K Banfield

Abstract

The mechanisms employed in the retention of Golgi resident membrane proteins are diverse and include features such as the composition and length of the protein's transmembrane domain and motifs that mediate direct or indirect associations with COPI-coatomer. However, in sum the current compendium of mechanisms cannot account for the localization of all Golgi membrane proteins, and this is particularly the case for proteins such as the glycosyltransferases. Here we describe a novel mechanism that mediates the steady-state retention of a subset of glycosyltransferases in the Golgi of budding yeast cells. This mechanism is mediated by a deubiquitinase complex composed of Bre5p and Ubp3p. We show that in the absence of this deubiquitinase certain glycosyltransferases are mislocalized to the vacuole, where they are degraded. We also show that Bre5p/Ubp3p clients bind to COPI-coatomer via a series of positively charged amino acids in their cytoplasmically exposed N-termini. Furthermore, we identify two proteins (Ktr3p and Mnn4p) that show a requirement for both Bre5p/Ubp3p as well as the COPI-coatomer-affiliated sorting receptor Vps74p. We also establish that some proteins show a nutrient-dependent role for Vps74p in their Golgi rete...Continue Reading

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Citations

Oct 29, 2020·Molecular Biology of the Cell·Gege Yang, David K Banfield
May 27, 2021·Archives of Biochemistry and Biophysics·Pablo Lujan, Felix Campelo
Aug 16, 2021·The Journal of Biological Chemistry·Nathan A Snyder, Gustavo M Silva

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Methods Mentioned

BETA
deubiquitination
glycosylation
and
fluorescence microscopy
GTPase
ubiquitination
pull-down

Software Mentioned

ImageJ
Adobe Photoshop

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