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Exploring the short linear motif-mediated protein-protein interactions of CrkL through ProP-PD.
Pagano, L; Simonetti, L; Pennacchietti, V; Toto, A; Malagrinò, F; Ivarsson, Y; Gianni, S.
Afiliación
  • Pagano L; Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Universita di Roma, Laboratory Affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185, Rome, Italy.
  • Simonetti L; Department of Chemistry - BMC, Husargatan 3, 751 23, Uppsala, Sweden.
  • Pennacchietti V; Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Universita di Roma, Laboratory Affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185, Rome, Italy.
  • Toto A; Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Universita di Roma, Laboratory Affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185, Rome, Italy.
  • Malagrinò F; Dipartimento di Medicina clinica, sanità pubblica, scienze della vita e dell'ambiente, Università dell'Aquila, Piazzale Salvatore Tommasi 1, L'Aquila, Coppito, 67010, Italy.
  • Ivarsson Y; Department of Chemistry - BMC, Husargatan 3, 751 23, Uppsala, Sweden. Electronic address: ylva.ivarsson@kemi.uu.se.
  • Gianni S; Dipartimento di Scienze Biochimiche "A. Rossi Fanelli", Sapienza Universita di Roma, Laboratory Affiliated to Istituto Pasteur Italia - Fondazione Cenci Bolognetti, 00185, Rome, Italy. Electronic address: stefano.gianni@uniroma1.it.
Biochem Biophys Res Commun ; 703: 149658, 2024 04 09.
Article en En | MEDLINE | ID: mdl-38387229
ABSTRACT
Adaptor proteins play a pivotal role in cellular signaling mediating a multitude of protein-protein interaction critical for cellular homeostasis. Dysregulation of these interactions has been linked to the onset of various cancer pathologies and exploited by viral pathogens during host cell takeover. CrkL is an adaptor protein composed of an N-terminal SH2 domain followed by two SH3 domains that mediate interactions with diverse partners through the recognition of specific binding motifs. In this study, we employed proteomic peptide-phage display (ProP-PD) to comprehensively explore the short linear motif (SLiM)-based interactions of CrkL. Furthermore, we scrutinized how the binding affinity for selected peptides was influenced in the context of the full-length CrkL versus the isolated N-SH3 domain. Importantly, our results provided insights into SLiM-binding sites within previously reported interactors, as well as revealing novel human and viral ligands, expanding our understanding of the interactions mediated by CrkL and highlighting the significance of SLiM-based interactions in mediating adaptor protein function, with implications for cancer and viral pathologies.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Mapeo de Interacción de Proteínas / Proteínas Adaptadoras Transductoras de Señales / Técnicas de Visualización de Superficie Celular Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2024 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Mapeo de Interacción de Proteínas / Proteínas Adaptadoras Transductoras de Señales / Técnicas de Visualización de Superficie Celular Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2024 Tipo del documento: Article País de afiliación: Italia Pais de publicación: Estados Unidos