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Titolo:
Cloning of human PRP4 reveals interaction with Clk1
Autore:
Kojima, T; Zama, T; Wada, K; Onogi, H; Hagiwara, M;
Indirizzi:
Tokyo Med & Dent Univ, Med Res Inst, Dept Funct Genom, Bunkyo Ku, Tokyo 1138510, Japan Tokyo Med & Dent Univ Tokyo Japan 1138510 unkyo Ku, Tokyo 1138510, Japan Keio Univ, Sch Med, Dept Med, Shinjuku Ku, Tokyo 1600016, Japan Keio UnivTokyo Japan 1600016 ept Med, Shinjuku Ku, Tokyo 1600016, Japan Tokai Univ, Sch Med, Inst Med Sci, Isehara, Kanagawa 2591193, Japan Tokai Univ Isehara Kanagawa Japan 2591193 sehara, Kanagawa 2591193, Japan Tokai Univ, Sch Med, Dept Med, Isehara, Kanagawa 2591193, Japan Tokai Univ Isehara Kanagawa Japan 2591193 sehara, Kanagawa 2591193, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 34, volume: 276, anno: 2001,
pagine: 32247 - 32256
SICI:
0021-9258(20010824)276:34<32247:COHPRI>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-SPECIFIC KINASE; SPLICING FACTOR SF2/ASF; FISSION YEAST; SCHIZOSACCHAROMYCES-POMBE; SR PROTEINS; CELL-CYCLE; INTRANUCLEAR DISTRIBUTION; SUBCELLULAR-LOCALIZATION; FUNCTIONAL-ANALYSIS; SERINE-RICH;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Hagiwara, M Tokyo Med & Dent Univ, Med Res Inst, Dept Funct Genom, Bunkyo Ku, 1-5-45 Yushima, Tokyo 1138510, Japan Tokyo Med & Dent Univ 1-5-45 Yushima Tokyo Japan 1138510 apan
Citazione:
T. Kojima et al., "Cloning of human PRP4 reveals interaction with Clk1", J BIOL CHEM, 276(34), 2001, pp. 32247-32256

Abstract

Prp4 is a protein kinase of Schizosaccharomyces pombe identified through its role in pre-mRNA splicing, and belongs to a kinase family including mammalian serine/arginine-rich protein-specific kinases and Clks, whose substrates are serine/arginine-rich proteins. We cloned human PRP4 (hPRP4) full-length cDNA and the antiserum raised against a partial peptide of hPRP4 recognized 170-kDa polypeptide in HeLa S3 cell extracts. Northern blot analysis revealed that hPRP4 mRNA was ubiquitously expressed in multiple tissues. The extended NH2-terminal region of hPRP4 contains an arginine/serine-rich domain and putative nuclear localization signals. hPRP4 phosphorylated and interacted with SF2/ASF, one of the essential splicing factors. Indirect immunofluorescence analysis revealed that endogenous hPRP4 was distributed in anuclear speckled pattern and colocalized with SF2/ASF in HeLa S3 cells. Furthermore, hPRP4 interacted directly with Clk1 on its COOH terminus, and the arginine/serine-rich domain of hPRP4 was phosphorylated by Clk1 in vitro. Overexpression of Clk1 caused redistribution of hPRP4, from the speckled to the diffuse pattern in nucleoplasm, whereas inactive mutant of Clk1 caused no change of hPRP4 localization. These findings suggest that the NH2-terminal region of hPRP4 may play regulatory roles under an unidentified signaltransduction pathway through Clk1.

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Documento generato il 06/04/20 alle ore 09:57:54