ArticleProceedings of the National Academy of Sciences of the United States of America1995
p115 is a general vesicular transport factor related to the yeast endoplasmic reticulum to Golgi transport factor Uso1p.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 199 citations in OpenAlex.
- The Golgi vesicle tether p115 can bind directly to the ER exit site organiser Sec16A.Journal of cell science · 2026Article
- The proximity interactome of PML isoforms I and II under fatty acid stress.FEBS letters · 2025Article
- Tailoring Tumor Cell Golgi Apparatus-Targeting Self-Assembled Peptide for Effective Immunotherapy via Reshaping MIF-Mediated Immunosuppressive Network.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Motor Function of the Two-Component EEA1-Rab5 Revealed by dcFCCS.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Characterization and functional analysis ofmBio · 2024Article
- Article
- RNAseq Analysis of FABP4 Knockout Mouse Hippocampal Transcriptome Suggests a Role for WNT/β-Catenin in Preventing Obesity-Induced Cognitive Impairment.International journal of molecular sciences · 2023Article
- SAYSD1 senses UFMylated ribosome to safeguard co-translational protein translocation at the endoplasmic reticulum.Cell reports · 2023Article
- Stress-induced phase separation of ERES components into Sec bodies precedes ER exit inhibition in mammalian cells.Journal of cell science · 2022Article
- Getting Sugar Coating Right! The Role of the Golgi Trafficking Machinery in Glycosylation.Cells · 2021Review
- A Novel 65-bp Indel in theAnimals : an open access journal from MDPI · 2020Article
- Membrane Tethering Potency of Rab-Family Small GTPases Is Defined by the C-Terminal Hypervariable Regions.Frontiers in cell and developmental biology · 2020Article
- The Golgi Apparatus May Be a Potential Therapeutic Target for Apoptosis-Related Neurological Diseases.Frontiers in cell and developmental biology · 2020Review
- HDAC6 Inhibition Protects against OGDR-Induced Golgi Fragmentation and Apoptosis.Oxidative medicine and cellular longevity · 2019Article
- The dense-core vesicle maturation protein CCCP-1 binds RAB-2 and membranes through its C-terminal domain.Traffic (Copenhagen, Denmark) · 2017Article
- Globozoospermia and lack of acrosome formation in GM130-deficient mice.Cell death & disease · 2017Article
- Golgb1 regulates protein glycosylation and is crucial for mammalian palate development.Development (Cambridge, England) · 2016Article
- Transport Vesicle Tethering at the Trans Golgi Network: Coiled Coil Proteins in Action.Frontiers in cell and developmental biology · 2016Review
- p115-SNARE interactions: a dynamic cycle of p115 binding monomeric SNARE motifs and releasing assembled bundles.Traffic (Copenhagen, Denmark) · 2015Article
- Rab family of GTPases.Methods in molecular biology (Clifton, N.J.) · 2015Review
24 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A recently discovered vesicular transport factor, termed p115, is required along with N-ethylmaleimide-sensitive fusion protein (NSF) and soluble NSF attachment proteins for in vitro Golgi transport. p115 is a peripheral membrane protein found predominantly on the Golgi. Biochemical and electron microscopic analyses indicate that p115 is an elongated homodimer with two globular "heads" and an extended "tail" reminiscent of myosin II. We have cloned and sequenced cDNAs for bovine and rat p115. The predicted translation products are 90% identical, and each can be divided into three domains. The predicted 108-kDa bovine protein consists of an N-terminal 73-kDa globular domain followed by a 29-kDa coiled-coil dimerization domain, a linker segment of 4 kDa, and a highly acidic domain of 3 kDa. p115 is related to Uso1p, a protein required for endoplasmic reticulum to Golgi vesicular transport in Saccharomyces cerevisiae, which has a similar "head-coil-acid" domain structure. The p115 and Uso1p heads are similar in size, have approximately 25% sequence identity, and possess two highly homologous regions (62% and 60% identity over 34 and 53 residues, respectively). There is a third region of homology (50% identity over 28 residues) between the coiled-coil and acidic domains. Although the acidic nature of the p115 and Uso1p C termini is conserved, the primary sequence is not. We discuss these results in light of the proposed function of p115 in membrane targeting and/or fusion.
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