ReviewFEBS letters2023
The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11.
Review in FEBS letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- Trappc4 is required for early mammalian development.Zygote (Cambridge, England) · 2026Article
- A subcomplex comprising TRAPPC11, TRAPPC12, TRAPPC13 and the fungal TRAPPC2L homolog, Tca17, directs TRAPPIII to autophagy.Journal of cell science · 2026Article
- The Golgi vesicle tether p115 can bind directly to the ER exit site organiser Sec16A.Journal of cell science · 2026Article
- The Human Autophagy Core Complexes.Annual review of biochemistry · 2026Review
- The Functions of RAB GTPases at the Golgi Complex.Sub-cellular biochemistry · 2026Review
- Guanine Nucleotide Exchange Factors and Small GTPases: Their Regulation and Functions, Diseases, and Therapeutic Targets.MedComm · 2025Review
- Structural insights into traffic through the Golgi complex.Current opinion in cell biology · 2025Review
- TRAPPopathies: Severe Multisystem Disorders Caused by Variants in Genes of the Transport Protein Particle (TRAPP) Complexes.International journal of molecular sciences · 2024Review
- Article
- Unveiling the TRAPP: The role of plant TRAPPII in adaptive growth decisions.The Journal of cell biology · 2024Article
- Article
- Biochemical Structure and Function of TRAPP Complexes in the Cardiac System.JACC. Basic to translational science · 2023Article
- Subcellular positioning during cell division and cell plate formation in maize.Frontiers in plant science · 2023Article
- Disease-Associated Factors at the Endoplasmic Reticulum-Golgi Interface.Traffic (Copenhagen, Denmark)Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Transport Protein Particle (TRAPP) complexes are highly conserved multisubunit complexes that act as nucleotide exchange factors (GEFs) for Rab GTPases. They act in both protein secretion and autophagy and have also been proposed to have a role in other processes such as cytokinesis and ciliogenesis. There are two TRAPP complexes in metazoans: TRAPPII, which activates Rab11; and TRAPPIII, which activates Rab1. Both complexes share a core of small subunits that form the active site for the exchange of GDP for GTP. In addition, each TRAPP complex has distinct large subunits that determine the specificity of each complex towards its substrate Rab and are essential for activity in vivo. Crystal structures have revealed the organisation of the TRAPP core and the mechanism of Rab1 activation, whilst recent cryo-EM structures have unveiled the arrangement of the specific subunits around the core to form each complex. Combining these findings with functional experiments has allowed the proposal of mechanisms for how the specificity of each complex towards their cognate Rab is determined and for the arrangement of these large complexes on the membrane.
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Registered trials
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.