Binding of cargo sorting signals to AP-1 enhances its association with ADP ribosylation factor 1–GTP
Open accessAbstract
The adaptor protein AP-1 is the major coat protein involved in the formation of clathrin-coated vesicles at the trans-Golgi network. The prevailing view is that AP-1 recruitment involves coincident binding to multiple low-affinity sites comprising adenosine diphosphate ribosylation factor 1 (Arf-1)–guanosine triphosphate (GTP), cargo sorting signals, and phosphoinositides. We now show that binding of cargo signal peptides to AP-1 induces a conformational change in its core domain that greatly enhances its interaction with Arf-1–GTP. In addition, we provide evidence for cross talk between the dileucine and tyrosine binding sites within the AP-1 core domain such that binding of a cargo signal to one site facilitates binding to the other site. The stable association of AP-1 with Arf-1–GTP, which is induced by cargo signals, would serve to provide sufficient time for adaptor polymerization and clathrin recruitment while ensuring the packaging of cargo molecules into the forming transport vesicles.
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Recruitment of AP-1 to the TGN is mediated by Arf1 and Arf4 small G proteins.
“The recruitment of AP-1 to the TGN is known to be mediated by Arf1 and Arf4 small G proteins (Stamnes and Rothman, 1993; Lee et al., 2008; Nakai et al., 2013)”
From Distinct anterograde trafficking pathways of BACE1 and amyloid precursor protein from the TGN and the regulation of amyloid-β production (2020) · cites this paper as Lee et al., 2008
The Introduction describes Arf-1 as a primary docking site in the initial recruitment of AP-1 to the TGN. The Results and discussion also report Arf-1-dependent AP-1 recruitment in a liposome assay. The passages do not support the claim’s additional attribution to Arf4 (searched: Arf4 recruitment AP-1 TGN). (LLM, conf=0.87)
Experimental — accuracy not yet measuredRecruitment of AP-1 to TGN membranes is regulated by Arf1 and Arf4 small G proteins.
“Given that the recruitment of AP-1 to TGN membranes has been reported to be regulated by both Arf1 (Stamnes and Rothman, 1993; Le Borgne and Hoflack, 1997; Lee et al., 2008) and Arf4 (Lowery et al., 2013; Nakai et al., 2013) small G proteins”
From Distinct anterograde trafficking pathways of BACE1 and amyloid precursor protein from the TGN and the regulation of amyloid-β production (2020) · cites this paper as Lee et al., 2008
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Research works printed but not linked: 22
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Tan, J. Z. A., Fourriere, L., Wang, J., Perez, F., Boncompain, G., & Gleeson, P. A. (2020) · Molecular Biology of the Cell · doi:10.1091/mbc.e19-09-0487 · Cited by 37 · see citing works
- Authors
- Lee, I., Doray, B., Govero, J., & Kornfeld, S.
- Affiliations
- Washington University in St. Louis (US)
- Corresponding author
- Kornfeld, Stuart
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2008-02-04
- Volume
- 180
- Issue
- 3
- Pages
- 467-472
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2234244
- OpenAlex
- W2061517276
- Cited by
- 53
- References
- 0
- Citations by year
- 2026: 4 · 2024: 1 · 2023: 3 · 2022: 2 · 2021: 1 · 2019: 4 · 2018: 3 · 2017: 2 · 2016: 1 · 2015: 2 · 2014: 3 · 2013: 7 · 2012: 5
- FWCI
- 2.04
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (R37CA008759, R01CA008759)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- clathrin-coated vesicles, trans-Golgi network, vesicle trafficking, dileucine motif, tyrosine motif, protein conformational change, phosphoinositides, Golgi transport
- MeSH terms
- Animals, Binding Sites, Cattle, Clathrin, Guanosine Triphosphate, Humans, Leucine, Polymers, Protein Binding, Protein Conformation, Subcellular Fractions, Tyrosine, Signal Transduction, Protein Structure, Tertiary, Transcription Factor AP-1, ADP-Ribosylation Factor 1, Protein Transport, Transport Vesicles, Clathrin-Coated Vesicles
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