A Complete Set of SNAREs in Yeast

  title={A Complete Set of SNAREs in Yeast},
  author={Lena Burri and Trevor J Lithgow},
Trafficking of cargo molecules through the secretory pathway relies on packaging and delivery of membrane vesicles. These vesicles, laden with cargo, carry integral membrane proteins that can determine with which target membrane the vesicle might productively fuse. The membrane fusion process is highly conserved in all eukaryotes and the central components driving membrane fusion events involved in vesicle delivery to target membranes are a set of integral membrane proteins called SNAREs. The… 

Phylogeny of the SNARE vesicle fusion machinery yields insights into the conservation of the secretory pathway in fungi

Although the SNARE repertoire of baker's yeast is highly conserved, the analysis reveals that it is more deviated than the ones of basal fungi, highlighting that the trafficking pathways of baker’s yeast are not only different to those in animal cells but also are somewhatDifferent to those of many other fungi.

Structural and functional studies on SNAREs-mediated membrane fusion

Three sets of SNARE proteins coming from yeast, plant and mammalian sources have been investigated and the information gathered will help to understand the molecular mechanism ofSNARE-induced membrane fusion.

Membrane Traffic: Vesicle Budding and Fusion

Tight control of the flux of membrane components through vesicle budding and fusion is essential to cellular organization, giving rise to subcellular compartments with distinct functions. Cargo is

New Perspectives on SNARE Function in the Yeast Minimal Endomembrane System

This article synthesizes what the authors know about the machinery mediating endocytic membrane fusion with this new model for yeast endomembrane function and integrates these new findings into a broader understanding of the endosomal trafficking machinery components across eukaryotes.

VPS45p as a Model System for Elucidation of SEC1/MUNC18 Protein Function: A Dissertation

The function of the endosomal SM protein Vps45p is investigated by analyzing its interactions with its cognate syntaxin Tlg2p and its role in SNARE assembly, and a second binding site on TlG2p that corresponds to the closed conformation is discovered.

Diverse Role of SNARE Protein Sec22 in Vesicle Trafficking, Membrane Fusion, and Autophagy

A detailed account of Sec22 function is provided, its domain structure is summarized, what is known about its localization to discrete membranes, its contributions in conventional and unconventional autophagy, and a variety of other roles across different cellular systems ranging from higher to lower eukaryotes are discussed.

Functions of SNAREs in intracellular membrane fusion and lipid bilayer mixing

Structural studies are revealing the mechanisms by which SNARES form complexes and interact with other proteins and it is now apparent that the SNARE transmembrane segment not only anchors the protein but engages in SNARE-SNARE interactions and plays an active role in fusion.

Intracellular Membrane Fusion

This chapter summarizes the current knowledge of the mechanisms of intracellular membrane fusion with particular emphasis on the structure, function and regulation of the N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein family.

Elucidation of the Role of the Exocyst Subunit Sec6p in Exocytosis: A Dissertation

This work showed that the interaction between the plasma membrane t-SNARE Sec9p and the yeast exocyst subunit Sec6p can be observed in vivo and designed point mutations to disrupt that interaction and suggested several hypotheses which should prove testable in the future.

Membrane trafficking in protozoa SNARE proteins, H+-ATPase, actin, and other key players in ciliates.

  • H. Plattner
  • Biology
    International review of cell and molecular biology
  • 2010



Compartmental specificity of cellular membrane fusion encoded in SNARE proteins

It is found that, to a marked degree, the pattern of membrane flow in the cell is encoded and recapitulated by its isolated SNARE proteins, as predicted by the SNARE hypothesis.

SNAREs and the secretory pathway-lessons from yeast.

  • H. Pelham
  • Biology
    Experimental cell research
  • 1999
Current knowledge of the yeast SNAREs is summarized and the picture of the secretory pathway that emerges from such studies is summarized.

Two syntaxin homologues in the TGN/endosomal system of yeast

Tlg1p and Tlg2p are described, which imply that the Golgi apparatus can function with a single syntaxin, Sed5p, and are required for efficient endocytosis and to maintain normal levels of TGN proteins.

Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic.

It is proposed that Vti1p, along with Ykt6p and perhaps Sft2p, acts as a retrograde v-SNARE capable of interacting with the cis-Golgi t- SNARE Sed5p.

The syntaxins

SUMMARY The SNARE hypothesis predicts that a family of SNAP receptors are localized to and function in diverse intracellular membrane compartments where membrane fusion processes take place.

Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane.

It is shown that in neuroendocrine PC12 cells, synaptobrevin is not directly incorporated into the target organelle, synaptic‐like vesicles, rather, it is first inserted into the endoplasmic reticulum (ER) membrane and is then transported via the Golgi apparatus.

Asymmetric Requirements for a Rab Gtpase and Snare Proteins in Fusion of Copii Vesicles with Acceptor Membranes

This work proposes the asymmetry in SNARE protein function is maintained by an asymmetric distribution and requirement for the Ypt1p GTPase in this fusion event and suggests a dynamic cycling of SNARE machinery between ER and Golgi compartments.

Geranylgeranylated Snares Are Dominant Inhibitors of Membrane Fusion

It is proposed that the mutant SNAREs are fusion proteins unable to catalyze fusion of the distal leaflets of the secretory vesicle and plasma membrane, and the inverted cone–shaped lipid lysophosphatidylcholine rescues secretion from SNARE mutant cells.