title: New insights into RSK activation and hematopoietic cancer.
abstract: The tyrosine kinase receptor FGFR3 is thought to play a role in hematopoietic malignancies. A new study in this issue of Cancer Cell identifies the serine/threonine kinase RSK2 as a key substrate of FGFR3 in human t(4;14)-positive multiple myeloma (MM) cells. Constitutively active FGFR3 directly phosphorylates RSK2 on Tyr529, which primes RSK2 for activation by the kinases ERK1 and ERK2 (ERK1/2). In turn, RSK2 activity plays an important role in the survival of FGFR3-expressing MM cells.
authors.affiliation: CNIO (Spanish National Cancer Center), Melchor Fernández Almagro, 3, E-28029 Madrid, Spain.
authors.forename: Ana
authors.initials: A
authors.lastname: Cuadrado
authors.forename: Angel R
authors.initials: AR
authors.lastname: Nebreda
mesh_terms: D004789:Enzyme Activation; D006801:Humans; D020935:MAP Kinase Signaling System; D008954:Models, Biological; D009101:Multiple Myeloma / Q000201:enzymology*; D010766:Phosphorylation; D051498:Receptor, Fibroblast Growth Factor, Type 3 / Q000378:metabolism / Q000502:physiology*; D038744:Ribosomal Protein S6 Kinases, 90-kDa / Q000037:antagonists & inhibitors / Q000378:metabolism*