ArticleJournal of cell science2012
Identification of a functional domain within the p115 tethering factor that is required for Golgi ribbon assembly and membrane trafficking.
Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Investigating byssus self-assembly ofMarine life science & technology · 2026Article
- MitoSNARE Assembly and Disassembly Factors Regulate Basal Autophagy and Aging inInternational journal of molecular sciences · 2023Article
- AtypicalScience advances · 2022Article
- COPII vesicles can affect the activity of antisense oligonucleotides by facilitating the release of oligonucleotides from endocytic pathways.Nucleic acids research · 2018Article
- Emerging Insights into the Roles of Membrane Tethers from Analysis of Whole Organisms: The Tip of an Iceberg?Frontiers in cell and developmental biology · 2016Review
- Coat/Tether Interactions-Exception or Rule?Frontiers in cell and developmental biology · 2016Review
- TFG clusters COPII-coated transport carriers and promotes early secretory pathway organization.The EMBO journal · 2015Article
- p115-SNARE interactions: a dynamic cycle of p115 binding monomeric SNARE motifs and releasing assembled bundles.Traffic (Copenhagen, Denmark) · 2015Article
- Aβ-induced Golgi fragmentation in Alzheimer's disease enhances Aβ production.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Membrane tethering.F1000prime reports · 2014Review
- Binding of the vesicle docking protein p115 to the GTPase Rab1b regulates membrane recruitment of the COPI vesicle coat.Cellular logistics · 2013Article
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8 authors at 3 institutions in 3 countries.
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Abstract
The tethering factor p115 (known as Uso1p in yeast) has been shown to facilitate Golgi biogenesis and membrane traffic in cells in culture. However, the role of p115 within an intact animal is largely unknown. Here, we document that depletion of p115 by using RNA interference (RNAi) in C. elegans causes accumulation of the 170 kD soluble yolk protein (YP170) in the body cavity and retention of the yolk receptor RME-2 in the ER and the Golgi within oocytes. Structure-function analyses of p115 have identified two homology regions (H1 and H2) within the N-terminal globular head and the coiled-coil 1 (CC1) domain as essential for p115 function. We identify a new C-terminal domain of p115 as necessary for Golgi ribbon formation and cargo trafficking. We show that p115 mutants that lack the fourth CC domain (CC4) act in a dominant-negative manner to disrupt Golgi and prevent cargo trafficking in cells containing endogenous p115. Furthermore, using RNAi of p115 and the subsequent transfection with p115 deletion mutants, we show that CC4 is necessary for Golgi ribbon formation and membrane trafficking in cells depleted of endogenous p115. p115 has been shown to bind a subset of ER-Golgi SNAREs through CC1 and CC4 domains (Shorter et al., 2002). Our findings show that CC4 is required for p115 function, and suggest that both the CC1 and the CC4 SNARE-binding motifs participate in p115-mediated membrane tethering.
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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.