title: KIS is a protein kinase with an RNA recognition motif.
abstract: Protein phosphorylation is involved at multiple steps of RNA processing and in the regulation of protein expression. We present here the first identification of a serine/threonine kinase that possesses an RNP-type RNA recognition motif: KIS. We originally isolated KIS in a two-hybrid screen through its interaction with stathmin, a small phosphoprotein proposed to play a general role in the relay and integration of diverse intracellular signaling pathways. Determination of the primary sequence of KIS shows that it is formed by the juxtaposition of a kinase core with little homology to known kinases and a C-terminal domain that contains a characteristic RNA recognition motif with an intriguing homology to the C-terminal motif of the splicing factor U2AF. KIS produced in bacteria has an autophosphorylating activity and phosphorylates stathmin on serine residues. It also phosphorylates in vitro other classical substrates such as myelin basic protein and synapsin but not histones that inhibit its autophosphorylating activity. Immunofluorescence and biochemical analyses indicate that KIS overexpressed in HEK293 fibroblastic cells is partly targetted to the nucleus. Altogether, these results suggest the implication of KIS in the control of trafficking and/or splicing of RNAs probably through phosphorylation of associated factors.
authors.affiliation: INSERM, U440, 17 rue du Fer à Moulin, 75005 Paris, France.
authors.forename: A
authors.initials: A
authors.lastname: Maucuer
authors.forename: S
authors.initials: S
authors.lastname: Ozon
authors.forename: V
authors.initials: V
authors.lastname: Manceau
authors.forename: O
authors.initials: O
authors.lastname: Gavet
authors.forename: S
authors.initials: S
authors.lastname: Lawler
authors.forename: P
authors.initials: P
authors.lastname: Curmi
authors.forename: A
authors.initials: A
authors.lastname: Sobel
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002451:Cell Compartmentation; D002467:Cell Nucleus / Q000201:enzymology; D003001:Cloning, Molecular; D003593:Cytoplasm / Q000201:enzymology; D004622:Embryo, Mammalian / Q000737:chemistry; D017403:In Situ Hybridization; D047908:Intracellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011487:Protein Conformation; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism*; D012323:RNA Processing, Post-Transcriptional; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D051381:Rats; D011994:Recombinant Proteins / Q000378:metabolism; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D014018:Tissue Distribution
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; D017346:Protein Serine-Threonine Kinases