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Identification of potential HDAC11 deacylase substrates by affinity pulldown MS.
Zhang, Yandong; Zhao, Qian; Lin, Hening.
Afiliación
  • Zhang Y; Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, United States.
  • Zhao Q; Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, United States.
  • Lin H; Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, United States; Howard Hughes Medical Institute, Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY, United States. Electronic address: hl379@cornell.edu.
Methods Enzymol ; 685: 43-55, 2023.
Article en En | MEDLINE | ID: mdl-37245910
Lysine fatty acylation is a protein posttranslational modification (PTM) that has been linked to various important biological processes. HDAC11, the sole member of class IV of histone deacetylases (HDACs), has been shown to have high lysine defatty-acylase activity. In order to better understand the functions of lysine fatty acylation and its regulation by HDAC11, it is important to identify the physiological substrates of HDAC11. This can be achieved through profiling the interactome of HDAC11 using a stable isotope labeling with amino acids in cell culture (SILAC) proteomics strategy. Here we describe a detailed method on using SILAC to identify the interactome of HDAC11. This method can be similarly used to identify the interactome, and thus potential substrates, of other PTM enzymes.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Histona Desacetilasas / Lisina Tipo de estudio: Diagnostic_studies Idioma: En Revista: Methods Enzymol Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Histona Desacetilasas / Lisina Tipo de estudio: Diagnostic_studies Idioma: En Revista: Methods Enzymol Año: 2023 Tipo del documento: Article País de afiliación: Estados Unidos
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