Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2019 Jul 26;8(8):780.
doi: 10.3390/cells8080780.

Stx5-Mediated ER-Golgi Transport in Mammals and Yeast

Peter Ta Linders  1 , Chiel van der Horst  1 , Martin Ter Beest  1 , Geert van den Bogaart  2   3
Affiliations
Review

Stx5-Mediated ER-Golgi Transport in Mammals and Yeast

Peter Ta Linders et al. Cells. .

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.

Keywords: Golgi apparatus; endoplasmic reticulum; membrane trafficking; secretory pathway; syntaxin 5.

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Schematic overview of the early secretory pathway in Saccharomyces cerevisiae (A) and mammalian cells (B). Abbreviations: ER, endoplasmic reticulum; ERES, endoplasmic reticulum exit sites; ERGIC, endoplasmic reticulum-Golgi intermediate compartment; MT, microtubule; MTOC, microtubule organizing center; TGN, trans-Golgi network.
Figure 2
Figure 2
Schematic overview of SNARE complexes of the early secretory pathway in Saccharomyces cerevisiae (A) and mammalian cells (B). The grey boxes indicate the known SNARE complexes and their location along the secretory pathway. Colors of the SNAREs: red, Qa-SNAREs; dark green, Qb-SNAREs; light green, Qc-SNAREs; blue, R-SNAREs. Abbreviations: ER, endoplasmic reticulum; ERGIC, endoplasmic reticulum-Golgi intermediate compartment; TGN, trans-Golgi network.
Figure 3
Figure 3
Conserved and distinct interactions of mammalian Stx5 and yeast Sed5p. Alignment of human (Hs) Stx5 and S. cerevisiae (Sc) Sed5p. Indicated are: the double arginine ER retrieval motif of the long isoform of Stx5 [49,57]; the alternative starting methionine of the short isoform of Stx5 [49]; the binding site to Scfd1 (mammals) and Sly1p (yeast) [60,61]; Sec24C/D binding site to the IxM motif of Stx5 [20,62]; Sec24p binding sites to the YNNSNPF motif (A-site) and LxxME motif (B-site) of Sed5p [63]; Caspase-3 cleavage site of Stx5 [64]; monoubiquitination site of Stx5 [65]; phosphorylation site of Sed5p [66].
Figure 4
Figure 4
Interactions of Stx5/Sed5p with Sec24 and Scfd1/Sly1p. (A) Crystal structure of yeast Sec24p (green) bound to the YNNSNPF motif of Sed5p (A-site) and the LxxME motif of Bet1p (B-site) [63]. Alignments of interacting regions of Sec24p with mammalian Sec24A–D are shown. Substrate-interacting residues are in bold and colored. Note that the A-site is not conserved, whereas the B-site seems conserved in mammalian Sec24A and B (not C and D). (B) Crystal structure of mammalian Sec24D (green) with the IxM motif of Stx5 (magenta; residues 241–248) [62]. Note that the IxM binding site is not conserved in mammalian Sec24A–D. (C) Conserved interactions between Stx5/Sed5p and Scfd1/Sly1p. Crystal structure of yeast Sly1p (orange) with the N-terminal region of Sed5p (magenta; residues 1–21) [61] aligned with an NMR structure of mammalian Scfd1 (yellow) [60]. Interacting residue F10 of the short isoform of Stx5 and Sed5p is indicated [60,61].
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Puthenveedu M.A., Linstedt A.D. Subcompartmentalizing the Golgi apparatus. Curr. Opin. Cell Biol. 2005;17:369–375. doi: 10.1016/j.ceb.2005.06.006. - DOI - PubMed
    1. Cottam N.P., Ungar D. Retrograde vesicle transport in the Golgi. Protoplasma. 2012;249:943–955. doi: 10.1007/s00709-011-0361-7. - DOI - PubMed
    1. Malsam J., Söllner T.H. Organization of SNAREs within the Golgi stack. Cold Spring Harb. Perspect. Biol. 2011;3:1–17. doi: 10.1101/cshperspect.a005249. - DOI - PMC - PubMed
    1. Papanikou E., Glick B.S. The yeast Golgi apparatus: Insights and mysteries. FEBS Lett. 2009;583:3746–3751. doi: 10.1016/j.febslet.2009.10.072. - DOI - PMC - PubMed
    1. Jackson C.L. Mechanisms of transport through the Golgi complex. J. Cell Sci. 2009;122:443–452. doi: 10.1242/jcs.032581. - DOI - PubMed

Publication types

MeSH terms

LinkOut - more resources