ArticleScientific reports2017
Crystal structure of Sec10, a subunit of the exocyst complex.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- The exocyst in ciliogenesis.Renal failure · 2025Review
- Sec10 negatively regulates antiviral immunity by downregulating NRF2-ATF4-RIG-I axis.International journal of biological sciences · 2025Article
- The exocyst in context.Biochemical Society transactions · 2024Review
- Emerging Roles of Exocyst Complex in Fungi: A Review.Journal of fungi (Basel, Switzerland) · 2024Review
- Structure of a membrane tethering complex incorporating multiple SNAREs.Nature structural & molecular biology · 2024Article
- Exocyst controls exosome biogenesis via Rab11a.Molecular therapy. Nucleic acids · 2022Article
- Homology and Modular Evolution of CATCHR at the Origin of the Eukaryotic Endomembrane System.Genome biology and evolution · 2021Article
- Integrative structure and function of the yeast exocyst complex.Protein science : a publication of the Protein Society · 2020Article
- The role of the exocyst in renal ciliogenesis, cystogenesis, tubulogenesis, and development.Kidney research and clinical practice · 2019Review
- The exocyst acting through the primary cilium is necessary for renal ciliogenesis, cystogenesis, and tubulogenesis.The Journal of biological chemistry · 2019Article
- Exposing the Elusive Exocyst Structure.Trends in biochemical sciences · 2018Review
- Cryo-EM structure of the exocyst complex.Nature structural & molecular biology · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The exocyst complex is a heterooctameric protein complex composed of Sec3, Sec5, Sec6, Sec8, Sec10, Sec15, Exo70 and Exo84. This complex plays an essential role in trafficking secretory vesicles to the plasma membrane through its interaction with phosphatidylinositol 4,5-bisphosphate and small GTPases. To date, the near-full-length structural information of each subunit has been limited to Exo70, although the C-terminal half structures of Sec6, Sec15 and Exo84 and the structures of the small GTPase-binding domains of Sec3, Sec5 and Exo84 have been reported. Here, we report the crystal structure of the near-full-length zebrafish Sec10 (zSec10) at 2.73 Å resolution. The structure of zSec10 consists of tandem antiparallel helix bundles that form a straight rod, like helical core regions of other exocyst subunits. This structure provides the first atomic details of Sec10, which may be useful for future functional and structural studies of this subunit and the exocyst complex.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.