What question did this study set out to answer?

The study aims to investigate the structural evolution of RPAP3 and its implications in various diseases.

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April 12, 2026Open Access

RPAP3: Structural Evolution, Chaperone Networks, and Disease Implications of a Transcriptional Co-Chaperone

Key Points

The study aims to investigate the structural evolution of RPAP3 and its implications in various diseases.
Analysis of RPAP3's structure and function in relation to its role as a chaperone.
Identification of interactions within chaperone networks.
Review of the implications of RPAP3 in disease mechanisms.
RPAP3 is shown to have significant evolutionary adaptations affecting its function.
Connections between RPAP3 and various chaperones reveal insights into disease pathways.
Altered RPAP3 activity is associated with several disease conditions, implying a potential target for intervention.

Abstract

Ataxia telangiectasia and Rad3-related protein; CHIP -Carboxyl terminus of Hsp70 interacting protein; CK2 -Casein kinase 2; DKC1 -Dyskerin Pseudouridine Synthase 1; DNA-PKc -DNA-dependent protein kinase catalytic subunit; DNAAF2 -Dynein axonemal assembly factor 2; DPCD -Deleted in primary ciliary dyskinesia; DYX1C1 -Dyslexia susceptibility 1 candidate gene 1 protein; EFTUD2 -Elongation factor Tu GTP binding domain containing 2; HK2 -Hexokinase 2; HOP -Hsp70-Hsp90 organizing protein; HSP90 -Heat shock protein 90; mTOR -Mammalian target of rapamycin; NAF1 -Nuclear assembly factor 1 ribonucleoprotein; NHP2 -Non-histone chromosome

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RPAP3: Structural Evolution, Chaperone Networks, and Disease Implications of a Transcriptional Co-Chaperone

Key Points

Abstract

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