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Proteomic profiling identifies a direct interaction between heat shock transcription factor 2 and the focal adhesion adapter talin-1.
Da Silva, Alejandro J; Hästbacka, Hendrik S E; Luoto, Jens C; Gough, Rosemarie E; Coelho-Rato, Leila S; Laitala, Leena M; Goult, Benjamin T; Imanishi, Susumu Y; Sistonen, Lea; Henriksson, Eva.
Afiliación
  • Da Silva AJ; Faculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland.
  • Hästbacka HSE; Turku Bioscience Centre, University of Turku and Åbo Akademi University, Turku, Finland.
  • Luoto JC; Faculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland.
  • Gough RE; Turku Bioscience Centre, University of Turku and Åbo Akademi University, Turku, Finland.
  • Coelho-Rato LS; Faculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland.
  • Laitala LM; Turku Bioscience Centre, University of Turku and Åbo Akademi University, Turku, Finland.
  • Goult BT; School of Biosciences, University of Kent, Canterbury, UK.
  • Imanishi SY; Faculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland.
  • Sistonen L; Turku Bioscience Centre, University of Turku and Åbo Akademi University, Turku, Finland.
  • Henriksson E; Faculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland.
FEBS J ; 2024 Sep 16.
Article en En | MEDLINE | ID: mdl-39285620
ABSTRACT
Heat shock factor 2 (HSF2) is a versatile transcription factor that regulates gene expression under stress conditions, during development, and in disease. Despite recent advances in characterizing HSF2-dependent target genes, little is known about the protein networks associated with this transcription factor. In this study, we performed co-immunoprecipitation coupled with mass spectrometry analysis to identify the HSF2 interactome in mouse testes, where HSF2 is required for normal sperm development. Endogenous HSF2 was discovered to form a complex with several adhesion-associated proteins, a finding substantiated by mass spectrometry analysis conducted in human prostate carcinoma PC-3 cells. Notably, this group of proteins included the focal adhesion adapter protein talin-1 (TLN1). Through co-immunoprecipitation and proximity ligation assays, we demonstrate the conservation of the HSF2-TLN1 interaction from mouse to human. Additionally, employing sequence alignment analyses, we uncovered a TLN1-binding motif in the HSF2 C terminus that binds directly to multiple regions of TLN1 in vitro. We provide evidence that the 25 C-terminal amino acids of HSF2, fused to EGFP, are sufficient to establish a protein complex with TLN1 and modify cell-cell adhesion in human cells. Importantly, this TLN1-binding motif is absent in the C-terminus of a closely related HSF family member, HSF1, which does not form a complex with TLN1. These results highlight the unique molecular characteristics of HSF2 in comparison to HSF1. Taken together, our data unveil the protein partners associated with HSF2 in a physiologically relevant context and identifies TLN1 as the first adhesion-related HSF2-interacting partner.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: FEBS J Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Finlandia Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Idioma: En Revista: FEBS J Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Finlandia Pais de publicación: Reino Unido