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
. 2012 Jul 1;2(3):151-160.
doi: 10.4161/cl.20490.

Vesicle trafficking from a lipid perspective: Lipid regulation of exocytosis in Saccharomyces cerevisiae

Jesper Johansen  1 , Vidhya Ramanathan, Christopher T Beh
Affiliations

Vesicle trafficking from a lipid perspective: Lipid regulation of exocytosis in Saccharomyces cerevisiae

Jesper Johansen et al. Cell Logist. .

Abstract

The protein cargo transported by specific types of vesicles largely defines the different secretory trafficking pathways operating within cells. However, mole per mole the most abundant cargo contained within transport vesicles is not protein, but lipid. Taking a "lipid-centric" point-of-view, we examine the importance of lipid signaling, membrane lipid organization and lipid metabolism for vesicle transport during exocytosis in budding yeast. In fact, the essential requirement for some exocytosis regulatory proteins can be bypassed by making simple manipulations of the lipids involved. During polarized exocytosis the sequential steps required to generate post-Golgi vesicles and target them to the plasma membrane (PM) involves the interplay of several types of lipids that are coordinately linked through PI4P metabolism and signaling. In turn, PI4P levels are regulated by PI4P kinases, the Sac1p PI4P phosphatase and the yeast Osh proteins, which are homologs of mammalian oxysterol-binding protein (OSBP). Together these regulators integrate the transitional steps required for vesicle maturation directly through changes in lipid composition and organization.

PubMed Disclaimer

Figures

None
Figure 1. Lipid-dependent events in yeast polarized exocytosis. During vesicle biogenesis (left) Sec14p-dependent regulation of lipid metabolism both stimulates DAG synthesis and inhibits DAG consumption as a precursor in PC production. As a precursor for the synthesis of PI-containing complex sphingolipids, PI is used in complex sphingolipid production at the expense of DAG production. Concentrated with sterols, de novo synthesized sphingolipids form membrane microdomains that recruit membrane proteins for exocytosis. In transit between the Golgi and PM (center), vesicles move along actin filaments propelled by a type V myosin (Myo2p). Myo2p interactions with vesicles is dependent in part on PI4P as is the reconfiguration of small GTPases (yellow) required for the assembly of vesicle-associated exocyst complex subunits (light red). At the interface between the PM and vesicle membrane (right), Rho GTPases and exocyst complex subunits associated with the PM (dark red) via PI(4,5)P2 assemble with the vesicle-bound exocyst complex subunits to facilitate vesicle docking at sites of polarized growth. Membrane fusion follows after v-SNAREs (tan) and t-SNAREs (blue) interactions.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Harsay E, Bretscher A. Parallel secretory pathways to the cell surface in yeast. J Cell Biol. 1995;131:297–310. doi: 10.1083/jcb.131.2.297. - DOI - PMC - PubMed
    1. Kearns BG, McGee TP, Mayinger P, Gedvilaite A, Phillips SE, Kagiwada S, et al. Essential role for diacylglycerol in protein transport from the yeast Golgi complex. Nature. 1997;387:101–5. doi: 10.1038/387101a0. - DOI - PMC - PubMed
    1. Henneberry AL, Lagace TA, Ridgway ND, McMaster CR. Phosphatidylcholine synthesis influences the diacylglycerol homeostasis required for SEC14p-dependent Golgi function and cell growth. Mol Biol Cell. 2001;12:511–20. - PMC - PubMed
    1. Skinner HB, McGee TP, McMaster CR, Fry MR, Bell RM, Bankaitis VA. The Saccharomyces cerevisiae phosphatidylinositol-transfer protein effects a ligand-dependent inhibition of choline-phosphate cytidylyltransferase activity. Proc Natl Acad Sci U S A. 1995;92:112–6. doi: 10.1073/pnas.92.1.112. - DOI - PMC - PubMed
    1. Routt SM, Bankaitis VA. Biological functions of phosphatidylinositol transfer proteins. Biochem Cell Biol. 2004;82:254–62. doi: 10.1139/o03-089. - DOI - PubMed

LinkOut - more resources