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A comprehensive overview to understand the dynamic R2SP complex.

ABSTRACT: Here, we used molecular biological, biochemical, biophysical and structural approaches to describe the human R2SP complex, that reveal similarities as well as significant differences compared to canonical R2TP and hints towards its specific mode of assembly and action. Cross-linking mass spectrometry experiments have been done on purified S'P dimer, R1R2:S'P complexes.

INSTRUMENT(S):

ORGANISM(S): Escherichia Coli

SUBMITTER: Hugo Gizardin-Fredon

LAB HEAD: Dr. Sarah Cianférani

PROVIDER: PXD056494 | Pride | 2026-02-13

REPOSITORIES: Pride

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			Action	DRS
	Files_IDs.xlsx	Xlsx
	QX16289LM.mgf	Mgf
	QX16289LM.raw	Raw
	QX16289LM.zhrm	Other
	QX16292LM.mgf	Mgf

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Publications

An integrative structural biology approach reveals the dynamic organization of the R2SP quaternary chaperone complex.

Santo Paulo E PE Chagot Marie-Eve ME Gizardin-Fredon Hugo H Ley Marie M Chenuel Thomas T Deslignière Evolène E Plassart Laura L Paiva Ana C F ACF Sousa Pedro M F PMF Bertrand Edouard E Charpentier Bruno B Verheggen Céline C Quinternet Marc M Meyer Philippe P Bandeiras Tiago M TM Cianférani Sarah S Plisson-Chastang Célia C Manival Xavier X

Nature communications 20260210

R2SP belongs to the R2TP-like quaternary chaperone family and consists of RUVBL1/RUVBL2 AAA+ ATPases, which powers the machinery, and SPAG1 and PIH1D2 adapter proteins that engage specific clients to promote their quaternary assembly. However, little is known about the structure of R2SP and the precise mode of action of these R2TP-like complexes. Here, we combined biochemical (ATPase and fluorescence polarization assays) and structural approaches (NMR, structural mass spectrometry, cryo-EM) to i ...[more]

PMID: 41667496

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