ArticleEukaryotic cell2005
Saccharomyces cerevisiae Rab-GDI displacement factor ortholog Yip3p forms distinct complexes with the Ypt1 Rab GTPase and the reticulon Rtn1p.
Article in Eukaryotic cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- ER sensing of lipid metabolism drives PRA family-dependent regulation of COPII vesicle transport.Nature communications · 2026Article
- Identification of atrial fibrillation-related genes through transcriptome data analysis and Mendelian randomization.Frontiers in cardiovascular medicine · 2024Article
- Evolution of factors shaping the endoplasmic reticulum.Traffic (Copenhagen, Denmark) · 2022Article
- Exploring the eukaryotic Yip and REEP/Yop superfamily of membrane-shaping adapter proteins (MSAPs): A cacophony or harmony of structure and function?Frontiers in molecular biosciences · 2022Review
- Di-arginine and FFAT-like motifs retain a subpopulation of PRA1 at ER-mitochondria membrane contact sites.PloS one · 2020Article
- Novel binding partners for Prenylated Rab Acceptor 1 identified by a split-ubiquitin yeast two-hybrid screen.BMC research notes · 2019Article
- Rab1a rescues the toxicity of PRAF3.Biochemistry and biophysics reports · 2018Article
- The RING-Type E3 Ligase XBAT35.2 Is Involved in Cell Death Induction and Pathogen Response.Plant physiology · 2017Article
- Rapid, optimized interactomic screening.Nature methods · 2015Article
- Guanine nucleotide exchange factors (GEFs) have a critical but not exclusive role in organelle localization of Rab GTPases.The Journal of biological chemistry · 2013Article
- Rab-GDI complex dissociation factor expressed through translational frameshifting in filamentous ascomycetes.PloS one · 2013Article
- An Arabidopsis prenylated Rab acceptor 1 isoform, AtPRA1.B6, displays differential inhibitory effects on anterograde trafficking of proteins at the endoplasmic reticulum.Plant physiology · 2011Article
- Localization of mRNAs coding for mitochondrial proteins in the yeast Saccharomyces cerevisiae.RNA (New York, N.Y.) · 2011Article
- Praf2 is a novel Bcl-xL/Bcl-2 interacting protein with the ability to modulate survival of cancer cells.PloS one · 2010Article
- Incorporating functional inter-relationships into protein function prediction algorithms.BMC bioinformatics · 2009Article
- ER membrane-bending proteins are necessary for de novo nuclear pore formation.The Journal of cell biology · 2009Article
- Article
- The reticulons: a family of proteins with diverse functions.Genome biology · 2007Review
- Extracellular regulators of axonal growth in the adult central nervous system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2006Review
- Rtn1p is involved in structuring the cortical endoplasmic reticulum.Molecular biology of the cell · 2006Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Rab GTPases are crucial regulators of organelle biogenesis, maintenance, and transport. Multiple Rabs are expressed in all cells, and each is localized to a distinct set of organelles, but little is known regarding the mechanisms by which Rabs are targeted to their resident organelles. Integral membrane proteins have been postulated to serve as receptors that recruit Rabs from the cytosol in a complex with the Rab chaperone, GDI, to facilitate the dissociation of Rab and GDI, hence facilitating loading of Rabs on membranes. We show here that the yeast (Saccharomyces cerevisiae) Golgi Rab GTPase Ypt1p can be copurified with the integral membrane protein Yip3p from detergent cell extracts. In addition, a member of the highly conserved reticulon protein family, Rtn1p, is also associated with Yip3p in vivo. However, Ypt1p did not copurify with Rtn1p, indicating that Yip3p is a component of at least two different protein complexes. Yip3p and Rtn1p are only partially colocalized in cells, with Yip3p localized predominantly to the Golgi and secondarily to the endoplasmic reticulum, whereas Rtn1p is localized predominantly to the endoplasmic reticulum and secondarily to the Golgi. Surprisingly, the intracellular localization of Rabs was not perturbed in yip3Delta or rtn1Delta mutants, suggesting that these proteins do not play a role in targeting Rabs to intracellular membranes. These data indicate that Yip3p may have multiple functions and that its interaction with Rabs is not critical for their recruitment to organelle membranes.
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