ArticleProceedings of the National Academy of Sciences of the United States of America2023
Oligomer-to-monomer transition underlies the chaperone function of AAGAB in AP1/AP2 assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- AP2: an indispensable host factor in virus infection.Journal of virology · 2026Review
- Regulation of AP1 adaptor assembly by the bi-handed chaperone MEA1.Nature communications · 2026Article
- Structural basis of pseudoGTPase-mediated protein-protein interactions.Structure (London, England : 1993) · 2025Article
- Bi-handed assembly chaperones regulate protein complex assembly through an intramolecular handover mechanism.Science advances · 2025Article
- An AAGAB-to-CCDC32 handover mechanism controls the assembly of the AP2 adaptor complex.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Assembly of protein complexes is facilitated by assembly chaperones. Alpha and gamma adaptin-binding protein (AAGAB) is a chaperone governing the assembly of the heterotetrameric adaptor complexes 1 and 2 (AP1 and AP2) involved in clathrin-mediated membrane trafficking. Here, we found that before AP1/2 binding, AAGAB exists as a homodimer. AAGAB dimerization is mediated by its C-terminal domain (CTD), which is critical for AAGAB stability and is missing in mutant proteins found in patients with the skin disease punctate palmoplantar keratoderma type 1 (PPKP1). We solved the crystal structure of the dimerization-mediating CTD, revealing an antiparallel dimer of bent helices. Interestingly, AAGAB uses the same CTD to recognize and stabilize the γ subunit in the AP1 complex and the α subunit in the AP2 complex, forming binary complexes containing only one copy of AAGAB. These findings demonstrate a dual role of CTD in stabilizing resting AAGAB and binding to substrates, providing a molecular explanation for disease-causing
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