Dataset.

Supporting Information for Adv. Sci., DOI 10.1002/advs.202105170 Identification of a New Cholesterol-Binding Site within the IFN-γ Receptor that is Required for Signal Transduction

Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/331452
Digital.CSIC. Repositorio Institucional del CSIC
  • Morana, Ornella
  • Nieto, Jon Ander
  • Björkholm, Patrik
  • Serna, Jorge Bernardino de la
  • Terrones, Oihana
  • Arboleya, Aroa
  • Ciceri, Dalila
  • Rojo, Iratxe
  • Blouin, Cédric M.
  • Lamaze, Christophe
  • Lorizate, Maier
  • Contreras, F. Xabier
20 pages. -- Figure S1. Bifunctional lipid probes and workflow used for in vivo photoaffinity binding studies. -- Figure S2. Photolabeling experiments of non-lipid nanodomain marker (transferrin receptor) and lipid nanodomain marker (Cav-1) with bifunctional lipids and competition experiments between bifunctional analogues and cold lipids in living cells. -- Figure S3. Role of previously described chol-binding motif in IFN-γR2-chol interaction in vivo. -- Figure S4. Physiochemical analysis of IFN-γR2TMD wild type and mutants. -- Figure S5. Validation of the novel chol-binding domain localized within the IFN-γR2TMD. -- Figure S6. Characterization of IFN-γR1 and IFN-γR2 constructs for ID-PRIME and proof of principle. -- Figure S7. Chol binding is required for IFN-γR transmembrane signal activation and PDL1 cell surface exposure in response to IFN-γ stimulation. -- Figure S8. Subcellular localization of candidate chol-binding proteins. -- Supplementary Table 1. Single-and Multi-span motifs found using MOPRO. -- Supplementary Table 2. List of chol-binding protein candidates., Peer reviewed
 
DOI: http://hdl.handle.net/10261/331452
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/331452

HANDLE: http://hdl.handle.net/10261/331452
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/331452
 
Ver en: http://hdl.handle.net/10261/331452
Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/331452

Digital.CSIC. Repositorio Institucional del CSIC
oai:digital.csic.es:10261/331452
Dataset. 2022

SUPPORTING INFORMATION FOR ADV. SCI., DOI 10.1002/ADVS.202105170 IDENTIFICATION OF A NEW CHOLESTEROL-BINDING SITE WITHIN THE IFN-Γ RECEPTOR THAT IS REQUIRED FOR SIGNAL TRANSDUCTION

Digital.CSIC. Repositorio Institucional del CSIC
  • Morana, Ornella
  • Nieto, Jon Ander
  • Björkholm, Patrik
  • Serna, Jorge Bernardino de la
  • Terrones, Oihana
  • Arboleya, Aroa
  • Ciceri, Dalila
  • Rojo, Iratxe
  • Blouin, Cédric M.
  • Lamaze, Christophe
  • Lorizate, Maier
  • Contreras, F. Xabier
20 pages. -- Figure S1. Bifunctional lipid probes and workflow used for in vivo photoaffinity binding studies. -- Figure S2. Photolabeling experiments of non-lipid nanodomain marker (transferrin receptor) and lipid nanodomain marker (Cav-1) with bifunctional lipids and competition experiments between bifunctional analogues and cold lipids in living cells. -- Figure S3. Role of previously described chol-binding motif in IFN-γR2-chol interaction in vivo. -- Figure S4. Physiochemical analysis of IFN-γR2TMD wild type and mutants. -- Figure S5. Validation of the novel chol-binding domain localized within the IFN-γR2TMD. -- Figure S6. Characterization of IFN-γR1 and IFN-γR2 constructs for ID-PRIME and proof of principle. -- Figure S7. Chol binding is required for IFN-γR transmembrane signal activation and PDL1 cell surface exposure in response to IFN-γ stimulation. -- Figure S8. Subcellular localization of candidate chol-binding proteins. -- Supplementary Table 1. Single-and Multi-span motifs found using MOPRO. -- Supplementary Table 2. List of chol-binding protein candidates., Peer reviewed




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