DPCD is a regulator of R2TP in ciliogenesis initiation through Akt signaling
Abstract
R2TP is a chaperone complex consisting of the AAA+ ATPases RUVBL1 and RUVBL2, as well as RPAP3 and PIH1D1 proteins. R2TP is responsible for the assembly of macromolecular complexes mainly acting through different adaptors. Using proximity-labeling mass spectrometry, we identified deleted in primary ciliary dyskinesia (DPCD) as an adaptor of R2TP. Here, we demonstrate that R2TP-DPCD influences ciliogenesis initiation through a unique mechanism by interaction with Akt kinase to regulate its phosphorylation levels rather than its stability. We further show that DPCD is a heart-shaped monomeric protein with two domains. A highly conserved region in the cysteine- and histidine-rich domains-containing proteins and SGT1 (CS) domain of DPCD interacts with the RUVBL2 DII domain with high affinity to form a stable R2TP-DPCD complex both in cellulo and in vitro. Considering that DPCD is one among several CS-domain-containing proteins found to associate with RUVBL1/2, we propose that RUVBL1/2 are CS-domain-binding proteins that regulate complex assembly and downstream signaling.
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BibTeX
@article{mao2026dpcd,
title = {{DPCD is a regulator of R2TP in ciliogenesis initiation through Akt signaling}},
author = {Yu-Qian Mao and Thiago Seraphim and Yimei Wan and Ruikai Wu and Etienne Coyaud and Muhammad Bin Munim and Antonio Mollica and Estelle Laurent and Mohan Babu and Vito Mennella and Brian Raught and Walid Houry},
journal = {Cell Reports},
year = {2026},
month = oct,
doi = {10.1016/j.celrep.2024.113713},
url = {https://hal.science/hal-05790874v1},
note = {CC BY-NC-ND},
}
RIS
TY - JOUR
TI - DPCD is a regulator of R2TP in ciliogenesis initiation through Akt signaling
AU - Yu-Qian Mao
AU - Thiago Seraphim
AU - Yimei Wan
AU - Ruikai Wu
AU - Etienne Coyaud
AU - Muhammad Bin Munim
AU - Antonio Mollica
AU - Estelle Laurent
AU - Mohan Babu
AU - Vito Mennella
AU - Brian Raught
AU - Walid Houry
PY - 2026
DA - 2026/10/10
JO - Cell Reports
DO - 10.1016/j.celrep.2024.113713
UR - https://hal.science/hal-05790874v1
AB - R2TP is a chaperone complex consisting of the AAA+ ATPases RUVBL1 and RUVBL2, as well as RPAP3 and PIH1D1 proteins. R2TP is responsible for the assembly of macromolecular complexes mainly acting through different adaptors. Using proximity-labeling mass spectrometry, we identified deleted in primary ciliary dyskinesia (DPCD) as an adaptor of R2TP. Here, we demonstrate that R2TP-DPCD influences ciliogenesis initiation through a unique mechanism by interaction with Akt kinase to regulate its phosphorylation levels rather than its stability. We further show that DPCD is a heart-shaped monomeric protein with two domains. A highly conserved region in the cysteine- and histidine-rich domains-containing proteins and SGT1 (CS) domain of DPCD interacts with the RUVBL2 DII domain with high affinity to form a stable R2TP-DPCD complex both in cellulo and in vitro. Considering that DPCD is one among several CS-domain-containing proteins found to associate with RUVBL1/2, we propose that RUVBL1/2 are CS-domain-binding proteins that regulate complex assembly and downstream signaling.
SN - 2211-1247
SN - 2211-1247
ER -