ArticleMolecular biology of the cell2013
A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- COG Complex in Golgi Trafficking and Glycosylation.Sub-cellular biochemistry · 2026Review
- Cytokine-Induced Cytotoxicity and Extracellular Matrix Abnormalities in Hepatocytes Derived From RAD50-Interacting Protein 1-Deficient Induced Pluripotent Stem Cells.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- A mysterious cause of recurrent acute liver dysfunction for over a decade.Gastroenterology report · 2022Article
- Golgi inCOGnito: From vesicle tethering to human disease.Biochimica et biophysica acta. General subjects · 2020Review
- RINT1 Loss Impairs Retinogenesis Through TRP53-Mediated Apoptosis.Frontiers in cell and developmental biology · 2020Article
- Maintaining order: COG complex controls Golgi trafficking, processing, and sorting.FEBS letters · 2019Review
- RINT1 Bi-allelic Variations Cause Infantile-Onset Recurrent Acute Liver Failure and Skeletal Abnormalities.American journal of human genetics · 2019Article
- Role of Alström syndrome 1 in the regulation of blood pressure and renal function.JCI insight · 2018Article
- Association of Human Papillomavirus 16 E2 with Rad50-Interacting Protein 1 Enhances Viral DNA Replication.Journal of virology · 2017Article
- Article
- Rint1 inactivation triggers genomic instability, ER stress and autophagy inhibition in the brain.Cell death and differentiation · 2016Article
- The Exocyst Subunit Sec6 Interacts with Assembled Exocytic SNARE Complexes.The Journal of biological chemistry · 2015Article
- How Rab proteins determine Golgi structure.International review of cell and molecular biology · 2015Review
- Membrane tethering.F1000prime reports · 2014Review
- Moonlighting functions of the NRZ (mammalian Dsl1) complex.Frontiers in cell and developmental biology · 2014Review
- Multipronged interaction of the COG complex with intracellular membranes.Cellular logistics · 2014Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Docking and fusion of transport vesicles/carriers with the target membrane involve a tethering factor-mediated initial contact followed by soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-catalyzed membrane fusion. The multisubunit tethering CATCHR family complexes (Dsl1, COG, exocyst, and GARP complexes) share very low sequence homology among subunits despite likely evolving from a common ancestor and participate in fundamentally different membrane trafficking pathways. Yeast Tip20, as a subunit of the Dsl1 complex, has been implicated in retrograde transport from the Golgi apparatus to the endoplasmic reticulum. Our previous study showed that RINT-1, the mammalian counterpart of yeast Tip20, mediates the association of ZW10 (mammalian Dsl1) with endoplasmic reticulum-localized SNARE proteins. In the present study, we show that RINT-1 is also required for endosome-to-trans-Golgi network trafficking. RINT-1 uncomplexed with ZW10 interacts with the COG complex, another member of the CATCHR family complex, and regulates SNARE complex assembly at the trans-Golgi network. This additional role for RINT-1 may in part reflect adaptation to the demand for more diverse transport routes from endosomes to the trans-Golgi network in mammals compared with those in a unicellular organism, yeast. The present findings highlight a new role of RINT-1 in coordination with the COG 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.