ArticleMolecular biology of the cell2011
C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking.
Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Who cites it
71 citing papers in PubMed.
- A protein interactome for the last eukaryotic common ancestor illuminates the biochemical basis of modern genetic diseases.Cell genomics · 2026Article
- Preclinical research in obesity-associated metabolic diseases using in vitro, multicellular, and non-mammalian models.Journal of physiology and biochemistry · 2025Review
- Effects of ER-phagy regulatory genes on the microenvironment of hepatocellular carcinoma: a comprehensive analysis.Discover oncology · 2025Article
- The TRAPPC8/TRS85 subunit of the Arabidopsis TRAPPIII tethering complex regulates endoplasmic reticulum function and autophagy.Plant physiology · 2025Article
- Biological Basis of Cell Trafficking: A General Overview.Journal of inherited metabolic disease · 2025Review
- Identification of gene-sun exposure interactions of GWAS-identified variants in perceived facial aging progression.Frontiers in aging · 2025Article
- Article
- TANGO2-related rhabdomyolysis symptoms are associated with abnormal autophagy functioning.Autophagy reports · 2024Article
- Ancient eukaryotic protein interactions illuminate modern genetic traits and disorders.bioRxiv : the preprint server for biology · 2024Article
- TRAPPC6B biallelic variants cause a neurodevelopmental disorder with TRAPP II and trafficking disruptions.Brain : a journal of neurology · 2024Article
- Biochemical Structure and Function of TRAPP Complexes in the Cardiac System.JACC. Basic to translational science · 2023Article
- Expanding the phenotypic spectrum ofJournal of medical genetics · 2023Article
- The TRAPP complexes: discriminating GTPases in context.FEBS letters · 2023Review
- The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11.FEBS letters · 2023Review
- TRAPPC1 is essential for the maintenance and differentiation of common myeloid progenitors in mice.EMBO reports · 2023Article
- Impact of interorganelle coordination between the conventional early secretory pathway and autophagy in cellular homeostasis and stress response.Frontiers in cell and developmental biology · 2023Review
- Further evidence of muscle involvement in neurodevelopmental disorder with epilepsy, spasticity, and brain atrophy.Annals of human genetics · 2022Article
- Mutation landscape of multiple myeloma measurable residual disease: identification of targets for precision medicine.Blood advances · 2022Article
- Genetic Parameter Estimation and Whole Sequencing Analysis of the Genetic Architecture of Chicken Keel Bending.Frontiers in genetics · 2022Article
- A novel homozygous variant inJournal of medical genetics · 2021Article
11 more citing papers are in PubMed but not listed here.
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6 authors.
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Abstract
TRAPP is a multisubunit tethering complex implicated in multiple vesicle trafficking steps in Saccharomyces cerevisiae and conserved throughout eukarya, including humans. Here we confirm the role of TRAPPC2L as a stable component of mammalian TRAPP and report the identification of four novel components of the complex: C4orf41, TTC-15, KIAA1012, and Bet3L. Two of the components, KIAA1012 and Bet3L, are mammalian homologues of Trs85p and Bet3p, respectively. The remaining two novel TRAPP components, C4orf41 and TTC-15, have no homologues in S. cerevisiae. With this work, human homologues of all the S. cerevisiae TRAPP proteins, with the exception of the Saccharomycotina-specific subunit Trs65p, have now been reported. Through a multidisciplinary approach, we demonstrate that the novel proteins are bona fide components of human TRAPP and implicate C4orf41 and TTC-15 (which we call TRAPPC11 and TRAPPC12, respectively) in ER-to-Golgi trafficking at a very early stage. We further present a binary interaction map for all known mammalian TRAPP components and evidence that TRAPP oligomerizes. Our data are consistent with the absence of a TRAPP I-equivalent complex in mammalian cells, suggesting that the fundamental unit of mammalian TRAPP is distinct from that characterized in S. cerevisiae.
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