Evidence map›Paper›PMID 40196695›Full record

ArticlebioRxiv : the preprint server for biology2025

A method for the detection and enrichment of endogenous cereblon substrates.

Hannah C Lloyd, Yuli Li, N Connor Payne, Zhenguang Zhao, Wenqing Xu, Alena Kroupova, David Zollman, Tengfang Long, Farah Kabir, Mei Chen and 7 more

Abstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

17 authors.

Hannah C LloydDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
Yuli LiDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
N Connor PayneDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
Zhenguang ZhaoDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
Wenqing XuDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.ORCID 0000-0001-7385-3141
Alena KroupovaCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee DD1 5JJ, UK.
David ZollmanCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee DD1 5JJ, UK.
Tengfang LongDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
Farah KabirDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
Mei ChenMass Spectrometry and Proteomics Resource (MSPRL), Division of Science, Faculty of Arts and Sciences, Harvard University, Cambridge, MA 02138, USA.
Rebecca FreemanDepartment of Stem Cell and Regenerative Biology, Harvard University and Harvard Stem Cell Institute, Cambridge, MA 02138, USA.
Ethan Yang FengDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
Sarah XiDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.
Ya-Chieh HsuDepartment of Stem Cell and Regenerative Biology, Harvard University and Harvard Stem Cell Institute, Cambridge, MA 02138, USA.
Alessio CiulliCentre for Targeted Protein Degradation, School of Life Sciences, University of Dundee, Dundee DD1 5JJ, UK.ORCID 0000-0002-8654-1670
Ralph MazitschekCenter for Systems Biology, Massachusetts General Hospital, Boston, MA 02114, USA.
Christina M WooDepartment of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.ORCID 0000-0001-8687-9105

Funding

Uncovering the substrate recognition mechanisms of the E3 ligase adaptor cereblonR01GM141406 · NIGMS · HARVARD UNIVERSITY · PI WOO, CHRISTINA · 2022 to 2025
$1.3M
Defining Sexual Dimorphism in the SkinF31AR083715 · NIAMS · HARVARD MEDICAL SCHOOL · PI FREEMAN, REBECCA JANE · 2024 to 2025
$80k
NIAMS NIH HHS F31 AR083715NIGMS NIH HHS R01 GM141406
6 · The paper itself

Abstract

C-Terminal cyclic imides are posttranslational modifications on proteins that are recognized and removed by the E3 ligase substrate adapter cereblon (CRBN). Despite the observation of these modifications across the proteome by mass spectrometry-based proteomics, an orthogonal and generalizable method to visualize the C-terminal cyclic imide would enhance detection, sensitivity, and throughput of endogenous CRBN substrate characterization. Here we develop an antibody-like reagent, termed "cerebody," for visualizing and enriching C-terminal cyclic imide-modified proteins. We describe the engineering of CRBN derivatives to produce cerebody and use it to identify CRBN substrates by Western blot and enrichment from whole cell and tissue lysates. CRBN substrates identified by cerebody enrichment are mapped, validated, and further characterized for dependence on the C-terminal cyclic imide modification. These methods will accelerate the characterization of endogenous CRBN substrates and their regulation.

Identifiers

PMID40196695
PMCPMC11974815

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