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Cited by 74Cellular transport and secretionExtracellular vesicles in diseaseLipid Membrane Structure and Behavior

Exposing the Elusive Exocyst Structure

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Lepore, Dante M., Martínez-Núñez, Leonora, Munson, Mary·2018·Trends in Biochemical Sciences
DOI 10.1016/j.tibs.2018.06.012PMC PMC6108956
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Abstract

A major challenge for a molecular understanding of membrane trafficking has been the elucidation of high-resolution structures of large, multisubunit tethering complexes that spatially and temporally control intracellular membrane fusion. Exocyst is a large hetero-octameric protein complex proposed to tether secretory vesicles at the plasma membrane to provide quality control of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-mediated membrane fusion. Breakthroughs in methodologies, including sample preparation, biochemical characterization, fluorescence microscopy, and single-particle cryoelectron microscopy, are providing critical insights into the structure and function of the exocyst. These studies now pose more questions than answers for understanding fundamental functional mechanisms, and they open wide the door for future studies to elucidate interactions with protein and membrane partners, potential conformational changes, and molecular insights into tethering reactions.

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  • RalA is a vesicle-bound small GTPase promoting exocytosis through interacting with the exocyst complex.

    “Reps1 and Ralbp1 form a binary complex that recognizes RalA, a vesicle-bound small guanosine triphosphatases (GTPase) promoting exocytosis through interacting with the exocyst complex.”

    From Regulation of cargo exocytosis by a Reps1-Ralbp1-RalA module (2023) · cites this paper as [8]

    The sections “What have we learned about the exocyst architecture and function?” and “Protein-protein interactions” identify RalA as a GTPase that interacts with exocyst subunits Exo84 and Sec5. They do not identify RalA as vesicle-bound; the vesicle-associated GTPase they name is Rab. The paper also says Ral–exocyst interactions may help control exocyst function, rather than establishing that RalA promotes exocytosis through that interaction. Page numbers were not available in our copy. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Research works printed but not linked: 82

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Authors
Lepore, D. M., Martínez-Núñez, L., & Munson, M.
Affiliations
University of Massachusetts Chan Medical School (US)
Corresponding author
Munson, Mary
ORCID
Venue
Trends in Biochemical Sciences
Publisher
Elsevier BV
Published
2018-09
Volume
43
Issue
9
Pages
714-725
ISSN
0968-0004 (ISSN-L)
DOI
10.1016/j.tibs.2018.06.012
PMC
PMC6108956
OpenAlex
W2884535761
Cited by
74
References
0
Citations by year
2026: 3 · 2025: 12 · 2024: 9 · 2023: 7 · 2022: 8 · 2021: 9 · 2020: 13 · 2019: 11 · 2018: 2
FWCI
0.99
Type
journal article
Language
en
Open access
Licence
Locations
  • Trends in Biochemical Sciences (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
National Institutes of Health (GM068803)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
Keywords
exocyst, tethering complexes, membrane trafficking, SNARE-mediated membrane fusion, protein complex structure, protein conformational change, membrane fusion
MeSH terms
Animals, Exocytosis, Humans, Membrane Fusion, SNARE Proteins, Exosomes

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