title: IRAK4 activation: a cautious embrace.
abstract: Structural and biochemical studies by Ferrao et al. (2014) in this issue demonstrate that dimerization of the kinase domain of IRAK4 is crucial for its activation, but with conditions: after-not before-receptor recruitment and before-not after-autophosphorylation.
authors.affiliation: Kimmel Center for Biology and Medicine at the Skirball Institute, New York University School of Medicine, New York, NY 10016, USA; Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY 10016, USA. Electronic address: stevan.hubbard@med.nyu.edu.
authors.forename: Stevan R
authors.initials: SR
authors.lastname: Hubbard
mesh_terms: D006801:Humans; D053592:Interleukin-1 Receptor-Associated Kinases / Q000737:chemistry* / Q000378:metabolism*; D053594:Myeloid Differentiation Factor 88 / Q000737:chemistry* / Q000378:metabolism*
chemical_list: C507779:MYD88 protein, human; D053594:Myeloid Differentiation Factor 88; C507773:IRAK4 protein, human; D053592:Interleukin-1 Receptor-Associated Kinases