Your browser doesn't support javascript.
loading
Proximity proteomics reveals role of Abelson interactor 1 in the regulation of TAK1/RIPK1 signaling.
Petersen, Max; Chorzalska, Anna; Pardo, Makayla; Rodriguez, Anaelena; Morgan, John; Ahsan, Nagib; Zhao, Ting C; Liang, Olin; Kotula, Leszek; Bertone, Paul; Gruppuso, Philip A; Dubielecka, Patrycja M.
Afiliación
  • Petersen M; Department of Medicine, Alpert Medical School, Brown University, Providence, RI, USA.
  • Chorzalska A; Division of Hematology/Oncology, Rhode Island Hospital, Providence, RI, USA.
  • Pardo M; Division of Biology and Medicine, Department of Pathology and Laboratory Medicine, Brown University, Providence, RI, USA.
  • Rodriguez A; Department of Medicine, Alpert Medical School, Brown University, Providence, RI, USA.
  • Morgan J; Division of Hematology/Oncology, Rhode Island Hospital, Providence, RI, USA.
  • Ahsan N; Department of Medicine, Alpert Medical School, Brown University, Providence, RI, USA.
  • Zhao TC; Division of Hematology/Oncology, Rhode Island Hospital, Providence, RI, USA.
  • Liang O; Department of Medicine, Alpert Medical School, Brown University, Providence, RI, USA.
  • Kotula L; Division of Hematology/Oncology, Rhode Island Hospital, Providence, RI, USA.
  • Bertone P; Flow Cytometry and Cell Sorting Core Facility, Roger Williams Medical Center, Providence, RI, USA.
  • Gruppuso PA; COBRE Center for Cancer Research Development, Proteomics Core Facility, Rhode Island Hospital, Providence, RI, USA.
  • Dubielecka PM; Department of Chemistry and Biochemistry, The University of Oklahoma, Norman, OK, USA.
Mol Oncol ; 17(11): 2356-2379, 2023 Nov.
Article en En | MEDLINE | ID: mdl-36635880
Dysregulation of the adaptor protein Abelson interactor 1 (ABI1) is linked to malignant transformation. To interrogate the role of ABI1 in cancer development, we mapped the ABI1 interactome using proximity-dependent labeling (PDL) with biotin followed by mass spectrometry. Using a novel PDL data filtering strategy, considering both peptide spectral matches and peak areas of detected peptides, we identified 212 ABI1 proximal interactors. These included WAVE2 complex components such as CYFIP1, NCKAP1, or WASF1, confirming the known role of ABI1 in the regulation of actin-polymerization-dependent processes. We also identified proteins associated with the TAK1-IKK pathway, including TAK1, TAB2, and RIPK1, denoting a newly identified function of ABI1 in TAK1-NF-κB inflammatory signaling. Functional assays using TNFα-stimulated, ABI1-overexpressing or ABI1-deficient cells showed effects on the TAK1-NF-kB pathway-dependent signaling to RIPK1, with ABI1-knockout cells being less susceptible to TNFα-induced, RIPK1-mediated, TAK1-dependent apoptosis. In sum, our PDL-based strategy enabled mapping of the ABI1 proximal interactome, thus revealing a previously unknown role of this adaptor protein in TAK1/RIPK1-based regulation of cell death and survival.
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Factor de Necrosis Tumoral alfa / Proteómica Límite: Humans Idioma: En Revista: Mol Oncol Asunto de la revista: BIOLOGIA MOLECULAR / NEOPLASIAS Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Factor de Necrosis Tumoral alfa / Proteómica Límite: Humans Idioma: En Revista: Mol Oncol Asunto de la revista: BIOLOGIA MOLECULAR / NEOPLASIAS Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos