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Titolo:
SRPK1 AND CLK STY PROTEIN-KINASES SHOW DISTINCT SUBSTRATE SPECIFICITIES FOR SERINE/ARGININE-RICH SPLICING FACTORS/
Autore:
COLWILL K; FENG LL; YEAKLEY JM; GISH GD; CACERES JF; PAWSON T; FU XD;
Indirizzi:
MT SINAI HOSP,SAMUEL LUNENFELD RES INST,PROGRAMME MOL BIOL & CANC,600UNIV AVE TORONTO ON M5G 1X5 CANADA MT SINAI HOSP,SAMUEL LUNENFELD RES INST,PROGRAMME MOL BIOL & CANC TORONTO ON M5G 1X5 CANADA UNIV TORONTO,DEPT MOL & MED GENET TORONTO ON M5S 1A8 CANADA UNIV CALIF SAN DIEGO,DIV CELLULAR & MOL MED SAN DIEGO CA 92093 COLD SPRING HARBOR LAB COLD SPRING HARBOR NY 11724
Titolo Testata:
The Journal of biological chemistry
fascicolo: 40, volume: 271, anno: 1996,
pagine: 24569 - 24575
SICI:
0021-9258(1996)271:40<24569:SACSPS>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA-BINDING PROTEINS; SR PROTEINS; SERINE-RICH; CONSERVED FAMILY; SITE SELECTION; CELL-CYCLE; SPLICEOSOME; IDENTIFICATION; REGULATORS; DOMAINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
K. Colwill et al., "SRPK1 AND CLK STY PROTEIN-KINASES SHOW DISTINCT SUBSTRATE SPECIFICITIES FOR SERINE/ARGININE-RICH SPLICING FACTORS/", The Journal of biological chemistry, 271(40), 1996, pp. 24569-24575

Abstract

Serine/arginine-rich (SR) proteins are essential for pre-mRNA splicing, and modify the choice of splice site during alternative splicing ina process apparently regulated by protein phosphorylation, Two protein kinases have been cloned that can phosphorylate SR proteins in vitro: SRPK1 and Clk/Sty. Here, we show that these two kinases phosphorylate the same SR proteins in. vitro, but that SRPK1 has the higher specific activity toward ASF/SF2. SRPK1, like Clk/Sty, phosphorylates ASF/SF2 in vitro on sites that are also phosphorylated in vivo. Tryptic peptide mapping of ASF/SF2 revealed that three of the phosphopeptides fromfull-length ASF/SF2 phosphorylated in vitro contain consecutive phosphoserine-arginine residues or phosphoserine-proline residues. In vitro, the Clk/Sty kinase phosphorylated Ser-Arg, Ser-Lys, or Ser-Pro sites, whereas SRPK1 had a strong preference for Ser-Arg sites. These results suggest that SRPK1 and Clk/Sty may play different roles in regulating SR splicing factors, and suggest that Clk/Sty has a broader substrate specificity than SRPK1.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/11/20 alle ore 06:59:16