ArticleThe Biochemical journal2005
The adaptor protein AP-4 as a component of the clathrin coat machinery: a morphological study.
Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Revealing the nervous system requirements of Alzheimer disease risk genes in Drosophila.American journal of human genetics · 2025Article
- Characterization of the malaria parasiteMicrobiology spectrum · 2025Article
- Endosomal traffic disorders: a driving force behind neurodegenerative diseases.Translational neurodegeneration · 2024Review
- Single-nucleus transcriptomes reveal spatiotemporal symbiotic perception and early response in Medicago.Nature plants · 2023Article
- Role of adaptin protein complexes in intracellular trafficking and their impact on diseases.Bioengineered · 2021Article
- Demonstration of correlative atomic force and transmission electron microscopy using actin cytoskeleton.Biophysics and physicobiology · 2017Article
- Adapting for endocytosis: roles for endocytic sorting adaptors in directing neural development.Frontiers in cellular neuroscience · 2015Review
- Article
- Expression and localization of silkworm adaptor protein complex-1 subunits, which were down-regulated post baculovirus infection.Molecular biology reports · 2012Article
- AP-1 and clathrin are essential for secretory granule biogenesis in Drosophila.Molecular biology of the cell · 2011Article
- Cell biology of membrane trafficking in human disease.International review of cytology · 2006Review
Corrections and comments
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Authors and funding
2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The four members of the AP (adaptor protein) family are heterotetrameric cytosolic complexes that are involved in the intracellular trafficking of cargo proteins between different organelles. They interact with motifs present in the cytoplasmic tails of their specific cargo proteins at different intracellular locations. While AP-1, AP-2 and AP-3 have been investigated extensively, very few studies have focused on the fourth member, AP-4. In the present study, we report on the intracellular localization of AP-4 in the MDCK (Madin-Darby canine kidney) and MelJuSo cell lines after immunogold labelling of ultrathin cryosections. We find that AP-4 is localized mainly in the Golgi complex, as well as on endosomes and transport vesicles. Interestingly, we show for the first time that AP-4 is localized with the clathrin coat machinery in the Golgi complex and in the endocytic pathway. Furthermore, we find that AP-4 is localized with the CI-MPR (cation-independent mannose 6-phosphate receptor), but not with the transferrin receptor, LAMP-2 (lysosomal-associated membrane protein-2) or invariant chain. The difference in morphology between CI-MPR/AP-4-positive vesicles and CI-MPR/AP-1-positive vesicles raises the possibility that AP-4 acts at a location different from that of AP-1 in the intracellular trafficking pathway of CI-MPR.
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