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PreprintCited by 20TGF-β signaling in diseasesDevelopmental Biology and Gene RegulationBiotin and Related Studies

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A versatile Halo- and SNAP-tagged BMP/TGFβ receptor library for quantification of cell surface ligand binding

Open access
Jatzlau, Jerome, Burdzinski, Wiktor, Trumpp, Michael, Obendorf, Leon, Roßmann, Kilian, Ravn, Katharina, Hyvönen, Marko, Bottanelli, Francesca, Broichhagen, Johannes, Knaus, Petra·2022·Communications Biology
DOI 10.1101/2022.03.04.482944PMC PMC9837045

Preprint — published as 10.1038/s42003-022-04388-4 · Paper page

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Abstract

The TGFβ superfamily of secreted growth factors comprises more than 30 members including TGFβs, BMPs and Activins. While all TGFβ superfamily members signal through heteromeric receptor complexes to regulate a plethora of developmental and homeostatic processes, each ligand possesses a unique affinity towards a subset of BMP and TGFβ type I and type II receptors. Whereas the Activin and TGFβ class display a higher affinity towards type II receptors, BMPs and GDFs preferentially bind to type I receptors. Sofar, the lack of specific antibodies and chemical biology tools hampered simultaneous testing of ligand binding towards all BMP and TGFβ receptors. Here we present a N-terminally Halo- and SNAP-tagged TGFβ/BMP receptor library to visualize the receptor complexes in dual color. In combination with novel fluorescently labeled TGFβ superfamily ligands, we established a Ligand Surface Binding Assay (LSBA) for optical quantification of receptor-dependent growth factor binding for Activin A, TGFβ1 and BMP9 in a cellular context. We confirm ligand-receptor interface specificity by identifying BMPR2- or ALK2-mutants that switch from a low-affinity Activin A- or BMP9-receptor to a high-affinity receptor, respectively.

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Metadata

Authors
Jatzlau, J., Burdzinski, W., Trumpp, M., Obendorf, L., Roßmann, K., Ravn, K., Hyvönen, M., Bottanelli, F., Broichhagen, J., & Knaus, P.
Affiliations
  • Leibniz-Forschungsinstitut für Molekulare Pharmakologie (DE)
  • University of Cambridge (GB)
  • Berlin-Brandenburger Centrum für Regenerative Therapien (DE)
Corresponding author
Knaus, Petra
ORCID
Venue
Communications Biology
Publisher
openRxiv
Published
2022-03-04
Volume
6
Issue
1
Pages
34-34
ISSN
2399-3642 (ISSN-L)
DOI
10.1101/2022.03.04.482944
PMC
PMC9837045
OpenAlex
W4315779629
Cited by
20
References
1
Citations by year
2026: 7 · 2025: 5 · 2024: 2 · 2023: 4 · 2022: 2
FWCI
1.60
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Communications Biology (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Refubium (Universitätsbibliothek der Freien Universität Berlin) (submittedVersion, cc-by)
  • Apollo (University of Cambridge) (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver (cc-by)
  • Apollo
  • Apollo (cc-by)
Funders
  • Deutsches Zentrum für Herz-Kreislaufforschung
  • Deutsche Forschungsgemeinschaft (SFB1444, SE2016/7-2, FOR 2165, SE2016/10-1, SFB 958)
  • Bundesministerium für Bildung und Forschung
  • Freie Universität Berlin
  • Berlin-Brandenburg School for Regenerative Therapies
  • Einstein Centrum für Regenerartive Therapien, Charité-Universitätsmedizin Berlin (SFB1444)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
Keywords
ligand-receptor binding, HaloTag, SNAP-tag, TGF-beta signaling, activin A, BMP9, TGF-β1, receptor signaling specificity, mutant screening, receptor evolution
MeSH terms
Ligands, Transforming Growth Factor beta, Receptors, Transforming Growth Factor beta, Bone Morphogenetic Proteins, Bone Morphogenetic Protein Receptors

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