ArticleThe Journal of biological chemistry2015
Bivalent Motif-Ear Interactions Mediate the Association of the Accessory Protein Tepsin with the AP-4 Adaptor Complex.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 citations in OpenAlex.
- The AP-4 accessory protein tepsin exhibits multivalent binding to LC3B.Advances in biological regulation · 2026Article
- Tepsin binds LC3B to promote ATG9A trafficking and delivery.Molecular biology of the cell · 2024Article
- Protein sorting from endosomes to the TGN.Frontiers in cell and developmental biology · 2023Review
- 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
- Proteomic characterization of isolated Arabidopsis clathrin-coated vesicles reveals evolutionarily conserved and plant-specific components.The Plant cell · 2022Article
- AP-4-mediated axonal transport controls endocannabinoid production in neurons.Nature communications · 2022Article
- 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
- Axonal autophagosome maturation defect through failure of ATG9A sorting underpins pathology in AP-4 deficiency syndrome.Autophagy · 2020Article
- Cargo Sorting at theCells · 2019Review
- 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
- Structure and evolution of ENTH and VHS/ENTH-like domains in tepsin.Traffic (Copenhagen, Denmark) · 2017Article
- Molecular Basis for the Interaction Between AP4 β4 and its Accessory Protein, Tepsin.Traffic (Copenhagen, Denmark) · 2016Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The heterotetrameric (ϵ-β4-μ4-σ4) complex adaptor protein 4 (AP-4) is a component of a non-clathrin coat involved in protein sorting at the trans-Golgi network (TGN). Considerable interest in this complex has arisen from the recent discovery that mutations in each of its four subunits are the cause of a congenital intellectual disability and movement disorder in humans. Despite its physiological importance, the structure and function of this coat remain poorly understood. To investigate the assembly of the AP-4 coat, we dissected the determinants of interaction of AP-4 with its only known accessory protein, the ENTH/VHS-domain-containing protein tepsin. Using a variety of protein interaction assays, we found that tepsin comprises two phylogenetically conserved peptide motifs, [GS]LFXG[ML]X[LV] and S[AV]F[SA]FLN, within its C-terminal unstructured region, which interact with the C-terminal ear (or appendage) domains of the β4 and ϵ subunits of AP-4, respectively. Structure-based mutational analyses mapped the binding site for the [GS]LFXG[ML]X[LV] motif to a conserved, hydrophobic surface on the β4-ear platform fold. Both peptide-ear interactions are required for efficient association of tepsin with AP-4, and for recruitment of tepsin to the TGN. The bivalency of the interactions increases the avidity of tepsin for AP-4 and may enable cross-linking of multiple AP-4 heterotetramers, thus contributing to the assembly of the AP-4 coat. In addition to revealing critical aspects of this coat, our findings extend the paradigm of peptide-ear interactions, previously established for clathrin-AP-1/AP-2 coats, to a non-clathrin coat.
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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.