The Exocyst at a Glance
Open accessAbstract
The exocyst is an octameric protein complex that is implicated in the tethering of secretory vesicles to the plasma membrane prior to SNARE-mediated fusion. Spatial and temporal control of exocytosis through the exocyst has a crucial role in a number of physiological processes, such as morphogenesis, cell cycle progression, primary ciliogenesis, cell migration and tumor invasion. In this Cell Science at a Glance poster article, we summarize recent works on the molecular organization, function and regulation of the exocyst complex, as they provide rationales to the involvement of this complex in such a diverse array of cellular processes.
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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 [7]
The Introduction (page not provided) identifies RalA as a Ral GTPase that interacts with the exocyst subunits Sec5 and Exo84, and links RalA–Sec5 engagement to exocytic trafficking. The passages do not establish that RalA is vesicle-bound. The separate statement about Reps1 and Ralbp1 is not the part attributed to this source. (LLM, conf=0.85)
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M-Sec promotes membrane nanotube formation by interacting with Ral and the exocyst complex
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- Authors
- Wu, B., & Guo, W.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Guo, Wei
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2015-01-01
- Volume
- 128
- Issue
- 16
- Pages
- 2957-64
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- PMC
- PMC4541039
- OpenAlex
- W2463928272
- Cited by
- 240
- References
- 1
- Citations by year
- 2026: 8 · 2025: 13 · 2024: 17 · 2023: 20 · 2022: 22 · 2021: 29 · 2020: 34 · 2019: 30 · 2018: 29 · 2017: 27 · 2016: 11
- FWCI
- 2.27
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Cell Science (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM111128, R01GM085146, GM085146, GM111128)
- 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 › Fungal and yeast genetics research
- Keywords
- exocyst complex, exocytosis, plasma membrane, morphogenesis, cell cycle progression, primary ciliogenesis, cell migration, tumor invasion, protein complex regulation
- MeSH terms
- Animals, Cell Cycle, Cell Membrane, Exocytosis, Humans, Membrane Fusion, Morphogenesis, rab GTP-Binding Proteins, ral Guanine Nucleotide Exchange Factor, Vesicular Transport Proteins, Membrane Fusion Proteins
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