ArticleScientific reports2017
Mammalian TRAPPIII Complex positively modulates the recruitment of Sec13/31 onto COPII vesicles.
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 24 papers.
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Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
- Trappc4 is required for early mammalian development.Zygote (Cambridge, England) · 2026Article
- Defective EV-mediated transport of SHH alters neural fate specification in EPM1 epilepsy.Science advances · 2026Article
- A subcomplex comprising TRAPPC11, TRAPPC12, TRAPPC13 and the fungal TRAPPC2L homolog, Tca17, directs TRAPPIII to autophagy.Journal of cell science · 2026Article
- Review
- The TRAPPC8/TRS85 subunit of the Arabidopsis TRAPPIII tethering complex regulates endoplasmic reticulum function and autophagy.Plant physiology · 2025Article
- Article
- Mea6/cTAGE5 cooperates with TRAPPC12 to regulate PTN secretion and white matter development.iScience · 2024Article
- Biochemical Structure and Function of TRAPP Complexes in the Cardiac System.JACC. Basic to translational science · 2023Article
- Novel Genetic and Phenotypic Expansion inGenes · 2023Article
- Large scale microfluidic CRISPR screening for increased amylase secretion in yeast.Lab on a chip · 2023Article
- 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
- Review
- Structural basis of TRAPPIII-mediated Rab1 activation.The EMBO journal · 2021Article
- TRIPP Is a Plant-Specific Component of the Arabidopsis TRAPPII Membrane Trafficking Complex with Important Roles in Plant Development.The Plant cell · 2020Article
- Broadly conserved roles of TMEM131 family proteins in intracellular collagen assembly and secretory cargo trafficking.Science advances · 2020Article
- Distinct Roles of TRAPPC8 and TRAPPC12 in Ciliogenesis via Their Interactions With OFD1.Frontiers in cell and developmental biology · 2020Article
- Deficiencies in vesicular transport mediated by TRAPPC4 are associated with severe syndromic intellectual disability.Brain : a journal of neurology · 2020Article
- Characterization of three TRAPPC11 variants suggests a critical role for the extreme carboxy terminus of the protein.Scientific reports · 2019Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Transport protein particle (TRAPP) complex is a tethering factor for COPII vesicle. Of three forms of TRAPP (TRAPPI, II and III) complexes identified so far, TRAPPIII has been largely considered to play a role in autophagy. While depletion of TRAPPIII specific subunits caused defects in the early secretory pathway and TRAPPIII might interact with components of the COPII vesicle coat, its exact role remains to be determined. In this study, we studied the function of TRAPPIII in early secretory pathway using a TRAPPIII-specific subunit, TRAPPC12, as starting point. We found that TRAPPC12 was localized to the ER exit sites and ERGIC. In cells deleted with TRAPPC12, ERGIC and to a lesser extent, the Golgi became dispersed. ER-to-Golgi transport was also delayed. TRAPPC12, but not TRAPPC8, bound to Sec13/Sec31A tetramer but each Sec protein alone could not interact with TRAPPC12. TRAPPIII positively modulated the assembly of COPII outer layer during COPII vesicle formation. These results identified a novel function of TRAPPIII as a positive modulator of the outer layer of the COPII coat.
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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.