Your browser doesn't support javascript.
loading
FAM150A and FAM150B are activating ligands for anaplastic lymphoma kinase.
Guan, Jikui; Umapathy, Ganesh; Yamazaki, Yasuo; Wolfstetter, Georg; Mendoza, Patricia; Pfeifer, Kathrin; Mohammed, Ateequrrahman; Hugosson, Fredrik; Zhang, Hongbing; Hsu, Amy W; Halenbeck, Robert; Hallberg, Bengt; Palmer, Ruth H.
Affiliation
  • Guan J; Department of Medical Biochemistry and Cell Biology, Instititute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Umapathy G; Department of Medical Biochemistry and Cell Biology, Instititute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Yamazaki Y; Department of Medical Biochemistry and Cell Biology, Instititute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Wolfstetter G; Department of Medical Biochemistry and Cell Biology, Instititute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Mendoza P; Department of Medical Biochemistry and Cell Biology, Instititute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Pfeifer K; Department of Medical Biochemistry and Cell Biology, Instititute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Mohammed A; Department of Medical Biochemistry and Cell Biology, Instititute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Hugosson F; Department of Medical Biochemistry and Cell Biology, Instititute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Zhang H; Five Prime Therapeutics Inc., South San Francisco, United States.
  • Hsu AW; Five Prime Therapeutics Inc., South San Francisco, United States.
  • Halenbeck R; Five Prime Therapeutics Inc., South San Francisco, United States.
  • Hallberg B; Department of Medical Biochemistry and Cell Biology, Instititute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Palmer RH; Department of Medical Biochemistry and Cell Biology, Instititute of Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
Elife ; 4: e09811, 2015 Sep 29.
Article in En | MEDLINE | ID: mdl-26418745
Aberrant activation of anaplastic lymphoma kinase (ALK) has been described in a range of human cancers, including non-small cell lung cancer and neuroblastoma (Hallberg and Palmer, 2013). Vertebrate ALK has been considered to be an orphan receptor and the identity of the ALK ligand(s) is a critical issue. Here we show that FAM150A and FAM150B are potent ligands for human ALK that bind to the extracellular domain of ALK and in addition to activation of wild-type ALK are able to drive 'superactivation' of activated ALK mutants from neuroblastoma. In conclusion, our data show that ALK is robustly activated by the FAM150A/B ligands and provide an opportunity to develop ALK-targeted therapies in situations where ALK is overexpressed/activated or mutated in the context of the full length receptor.
Subject(s)
Key words

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cytokines / Receptor Protein-Tyrosine Kinases / Enzyme Activation Limits: Humans Language: En Journal: Elife Year: 2015 Document type: Article Affiliation country: Suecia Country of publication: Reino Unido

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cytokines / Receptor Protein-Tyrosine Kinases / Enzyme Activation Limits: Humans Language: En Journal: Elife Year: 2015 Document type: Article Affiliation country: Suecia Country of publication: Reino Unido