ArticleTraffic (Copenhagen, Denmark)2016
Molecular Basis for the Interaction Between AP4 β4 and its Accessory Protein, Tepsin.
Article in Traffic (Copenhagen, Denmark), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- The AP-4 accessory protein tepsin exhibits multivalent binding to LC3B.Advances in biological regulation · 2026Article
- Tepsin and AP4 mediate transport from the trans-Golgi to the plant-like vacuole in toxoplasma.The Journal of cell biology · 2025Article
- Characterization of the malaria parasiteMicrobiology spectrum · 2025Article
- Pre-clinical development of AP4B1 gene replacement therapy for hereditary spastic paraplegia type 47.EMBO molecular medicine · 2024Article
- Tepsin binds LC3B to promote ATG9A trafficking and delivery.Molecular biology of the cell · 2024Article
- AP-4 loss in CRISPR-edited zebrafish affects early embryo development.Advances in biological regulation · 2023Article
- The adaptor protein chaperone AAGAB stabilizes AP-4 complex subunits.Molecular biology of the cell · 2022Article
- AP-4-mediated axonal transport controls endocannabinoid production in neurons.Nature communications · 2022Article
- Role of adaptin protein complexes in intracellular trafficking and their impact on diseases.Bioengineered · 2021Article
- EPSIN1 and MTV1 define functionally overlapping but molecularly distinctProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Integrating structural and evolutionary data to interpret variation and pathogenicity in adapter protein complex 4.Protein science : a publication of the Protein Society · 2020Article
- The FTS-Hook-FHIP (FHF) complex interacts with AP-4 to mediate perinuclear distribution of AP-4 and its cargo ATG9A.Molecular biology of the cell · 2020Article
- Cargo Sorting at theCells · 2019Review
- MUDENG Expression Profiling in Cohorts and Brain Tumor Biospecimens to Evaluate Its Role in Cancer.Frontiers in genetics · 2019Article
- AP-4 vesicles contribute to spatial control of autophagy via RUSC-dependent peripheral delivery of ATG9A.Nature communications · 2018Article
- Evolutionary origins and specialisation of membrane transport.Current opinion in cell biology · 2018Review
- AP-4 mediates export of ATG9A from theProceedings of the National Academy of Sciences of the United States of America · 2017Article
- [Advances in genetic research of cerebral palsy].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2017Review
- Structure and evolution of ENTH and VHS/ENTH-like domains in tepsin.Traffic (Copenhagen, Denmark) · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 4 countries.
Funding
Abstract
The adaptor protein 4 (AP4) complex (ϵ/β4/μ4/σ4 subunits) forms a non-clathrin coat on vesicles departing the trans-Golgi network. AP4 biology remains poorly understood, in stark contrast to the wealth of molecular data available for the related clathrin adaptors AP1 and AP2. AP4 is important for human health because mutations in any AP4 subunit cause severe neurological problems, including intellectual disability and progressive spastic para- or tetraplegias. We have used a range of structural, biochemical and biophysical approaches to determine the molecular basis for how the AP4 β4 C-terminal appendage domain interacts with tepsin, the only known AP4 accessory protein. We show that tepsin harbors a hydrophobic sequence, LFxG[M/L]x[L/V], in its unstructured C-terminus, which binds directly and specifically to the C-terminal β4 appendage domain. Using nuclear magnetic resonance chemical shift mapping, we define the binding site on the β4 appendage by identifying residues on the surface whose signals are perturbed upon titration with tepsin. Point mutations in either the tepsin LFxG[M/L]x[L/V] sequence or in its cognate binding site on β4 abolish in vitro binding. In cells, the same point mutations greatly reduce the amount of tepsin that interacts with AP4. However, they do not abolish the binding between tepsin and AP4 completely, suggesting the existence of additional interaction sites between AP4 and tepsin. These data provide one of the first detailed mechanistic glimpses at AP4 coat assembly and should provide an entry point for probing the role of AP4-coated vesicles in cell biology, and especially in neuronal function.
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Registered trials
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.