Cryo-EM reveals the architecture of the PELP1-WDR18 molecular scaffold

Jacob Gordon; Fleur L. Chapus; Elizabeth G. Viverette; Jason G. Williams; Leesa J. Deterding; Juno M. Krahn; Mario J. Borgnia; Joseph Rodriguez; Alan J. Warren; Robin E. Stanley

doi:10.1038/s41467-022-34610-0

Nature Communications (Nov 2022)

Cryo-EM reveals the architecture of the PELP1-WDR18 molecular scaffold

Jacob Gordon,
Fleur L. Chapus,
Elizabeth G. Viverette,
Jason G. Williams,
Leesa J. Deterding,
Juno M. Krahn,
Mario J. Borgnia,
Joseph Rodriguez,
Alan J. Warren,
Robin E. Stanley

Affiliations

Jacob Gordon: Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, 111 T. W. Alexander Drive
Fleur L. Chapus: Epigenetics and Stem Cell Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, 111 T. W. Alexander Drive
Elizabeth G. Viverette: Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, 111 T. W. Alexander Drive
Jason G. Williams: Epigenetics and Stem Cell Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, 111 T. W. Alexander Drive
Leesa J. Deterding: Epigenetics and Stem Cell Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, 111 T. W. Alexander Drive
Juno M. Krahn: Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, 111 T. W. Alexander Drive
Mario J. Borgnia: Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, 111 T. W. Alexander Drive
Joseph Rodriguez: Epigenetics and Stem Cell Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, 111 T. W. Alexander Drive
Alan J. Warren: Cambridge Institute for Medical Research, Cambridge Biomedical Campus, Keith Peters Building
Robin E. Stanley: Signal Transduction Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services, 111 T. W. Alexander Drive

DOI: https://doi.org/10.1038/s41467-022-34610-0
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 15

Abstract

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PELP1 is a large scaffolding protein implicated in many cellular activities, including ribosome assembly as part of the Rix1 complex, comprising PELP1, WDR18, TEX10 and other components. Here, authors present the cryo-EM structure of PELP1 in complex with its binding partner WDR18, revealing the architecture of PELP1's numerous signaling motifs.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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