ReviewFrontiers in cell and developmental biology2016
TRAPP Complexes in Secretion and Autophagy.
Review in Frontiers in cell and developmental biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed.
- Vitamin B6 Modifies Tau-Induced Cellular Stress- and Proteostasis-Related Responses.Journal of fungi (Basel, Switzerland) · 2026Article
- Alpha-cell glucagon is essential for maintaining β-cell function and identity in adult mice.The Journal of biological chemistry · 2026Article
- A protein interactome for the last eukaryotic common ancestor illuminates the biochemical basis of modern genetic diseases.Cell genomics · 2026Article
- Structural insights into predicted protein-protein interactions and protein complexes in the human proteome.Scientific reports · 2026Article
- The autophagy-specific exocyst subcomplex contributes to phagophore assembly site integrity by promoting phagophore expansion.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Genome-wide identification of modulators of Chlamydia trachomatis parasitophorous vacuole stability highlights an important role for sphingolipid supply.PLoS biology · 2025Article
- TRAPPC2l Participates in Male Germ Cell Development by Regulating Cell Division.Cell proliferation · 2025Article
- Selective clearance of aberrant membrane proteins by TORC1-mediated micro-ER-phagy.Cell reports · 2025Article
- Permanent cilia loss during cerebellar granule cell neurogenesis involves withdrawal of cilia maintenance and centriole capping.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- TRAPPopathies: Severe Multisystem Disorders Caused by Variants in Genes of the Transport Protein Particle (TRAPP) Complexes.International journal of molecular sciences · 2024Review
- Transcriptome-based network analysis related to regulatory T cells infiltration identified RCN1 as a potential biomarker for prognosis in clear cell renal cell carcinoma.BioData mining · 2024Article
- Visualization of ER-to-Golgi trafficking of procollagen X.Cell structure and function · 2024Article
- Protein overexpression by adeno-associated virus-based gene therapy products in cardiomyocytes induces endoplasmic reticulum stress and myocardial degeneration in mice.Journal of toxicologic pathology · 2024Article
- Article
- Ancient eukaryotic protein interactions illuminate modern genetic traits and disorders.bioRxiv : the preprint server for biology · 2024Article
- Regulation of adaptive growth decisions via phosphorylation of the TRAPPII complex in Arabidopsis.The Journal of cell biology · 2024Article
- ATG9 resides on a unique population of small vesicles in presynaptic nerve terminals.Autophagy · 2024Article
- Analysis ofVeterinary sciences · 2024Article
- Biochemical Structure and Function of TRAPP Complexes in the Cardiac System.JACC. Basic to translational science · 2023Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors.
Funding
Abstract
TRAPP is a highly conserved modular multi-subunit protein complex. Originally identified as a "transport protein particle" with a role in endoplasmic reticulum-to-Golgi transport, its multiple subunits and their conservation from yeast to humans were characterized in the late 1990s. TRAPP attracted attention when it was shown to act as a Ypt/Rab GTPase nucleotide exchanger, GEF, in the 2000s. Currently, three TRAPP complexes are known in yeast, I, II, and III, and they regulate two different intracellular trafficking pathways: secretion and autophagy. Core TRAPP contains four small subunits that self assemble to a stable complex, which has a GEF activity on Ypt1. Another small subunit, Trs20/Sedlin, is an adaptor required for the association of core TRAPP with larger subunits to form TRAPP II and TRAPP III. Whereas the molecular structure of the core TRAPP complex is resolved, the architecture of the larger TRAPP complexes, including their existence as dimers and multimers, is less clear. In addition to its Ypt/Rab GEF activity, and thereby an indirect role in vesicle tethering through Ypt/Rabs, a direct role for TRAPP as a vesicle tether has been suggested. This idea is based on TRAPP interactions with vesicle coat components. While much of the basic information about TRAPP complexes comes from yeast, mutations in TRAPP subunits were connected to human disease. In this review we will summarize new information about TRAPP complexes, highlight new insights about their function and discuss current controversies and future perspectives.
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