ArticleScience advances2025
Bi-handed assembly chaperones regulate protein complex assembly through an intramolecular handover mechanism.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- Differential Interactions of Tissue-Restricted Host Proteins SPLUNC1 and VAMP8 with VP3 of Human Bocaviruses 1 and 2.Pathogens (Basel, Switzerland) · 2026Article
- 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
A critical yet challenging step in protein complex assembly is the formation of a dimeric intermediate that serves as a seed for incorporating additional subunits. We hypothesized that this step could be facilitated by "bi-handed" chaperones that recognize two different subunits through distinct domains (hands). However, whether such chaperones exist remained unknown. Here, we identify AAGAB as a bona fide bi-handed chaperone. AAGAB uses its C-terminal domain (CTD) to bind the α subunit and its GTPase-like domain (GD) to bind the σ2 subunit of the AP2 adaptor complex, a central player in membrane trafficking. AAGAB first recruits α via its CTD; σ2 then joins through interaction with α, forming a conformationally immature α:σ2 hemicomplex at the CTD. This hemicomplex is subsequently transferred to the GD via a GD:σ2 binding interface, accompanied by conformational maturation. These findings establish AAGAB as the founding member of a bi-handed chaperone family and reveal an intramolecular handover mechanism that underlies their mode of action.
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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 Socratic graph.