ArticleNature communications2026
Regulation of AP1 adaptor assembly by the bi-handed chaperone MEA1.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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.
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8 authors.
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Abstract
Bidirectional trafficking between the trans-Golgi network (TGN) and endolysosomal compartments lies at the intersection of biosynthetic and degradative pathways. At the center of this trafficking route is the adaptor protein complex 1 (AP1), a heterotetramer essential for cargo recognition and vesicle budding. Here, we identified Male-Enhanced Antigen 1 (MEA1), a previously uncharacterized protein, as a critical AP1 regulator. Loss of MEA1 resulted in depletion of AP1 subunits and impaired trafficking of AP1-dependent cargoes. Mechanistically, MEA1 acts as a bi-handed chaperone, simultaneously engaging and stabilizing the μ1 and β1 subunits of AP1. The MEA1-stabilized μ1 and β1 collide with the γ and σ1 subunits stabilized by Alpha- and Gamma-Adaptin Binding Protein (AAGAB), another bi-handed chaperone, leading to formation of the tetrameric AP1 adaptor and release of both chaperones. These findings identify MEA1 as a key AP1 regulator and uncover a dual chaperone collision mechanism potentially generalizable to multiprotein complex assembly.
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