Stx5-Mediated ER-Golgi Transport in Mammals and Yeast

Cells
Peter Ta LindersGeert van den Bogaart

Abstract

The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) syntaxin 5 (Stx5) in mammals and its ortholog Sed5p in Saccharomyces cerevisiae mediate anterograde and retrograde endoplasmic reticulum (ER)-Golgi trafficking. Stx5 and Sed5p are structurally highly conserved and are both regulated by interactions with other ER-Golgi SNARE proteins, the Sec1/Munc18-like protein Scfd1/Sly1p and the membrane tethering complexes COG, p115, and GM130. Despite these similarities, yeast Sed5p and mammalian Stx5 are differently recruited to COPII-coated vesicles, and Stx5 interacts with the microtubular cytoskeleton, whereas Sed5p does not. In this review, we argue that these different Stx5 interactions contribute to structural differences in ER-Golgi transport between mammalian and yeast cells. Insight into the function of Stx5 is important given its essential role in the secretory pathway of eukaryotic cells and its involvement in infections and neurodegenerative diseases.

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Citations

Oct 6, 2020·Frontiers in Cell and Developmental Biology·Qiang HeWei Lu
Jul 8, 2020·International Journal of Molecular Sciences·Peter T A LindersGeert van den Bogaart
Feb 23, 2020·Nature Chemical Biology·Hesso Farhan
Oct 6, 2020·Frontiers in Cell and Developmental Biology·Shuwen DengWei Lu
Aug 5, 2020·Cytoskeleton·Wei SunYao-Chun Wang
Aug 14, 2020·Molecular & Cellular Proteomics : MCP·Molly M HanniganChristopher V Nicchitta
Feb 10, 2021·Cell & Bioscience·Qingchun LuLing Yang
Dec 19, 2020·Cell Death and Differentiation·Giulia CerratoGuido Kroemer

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Datasets Mentioned

BETA
GM130

Methods Mentioned

BETA
gene knockout
electron microscopy
glycosylation
immunoprecipitation
ubiquitination

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