TAILIEUCHUNG - Báo cáo khoa học: Phosphorylation of the Saccharomyces cerevisiae Grx4p glutaredoxin by the Bud32p kinase unveils a novel signaling pathway involving Sch9p, a yeast member of the Akt / PKB subfamily

TheSaccharomyces cerevisiaeatypical protein kinase Bud32p is a member of the nuclear endopeptidase-like, kinase, chromatin-associated⁄kinase, endopeptidase-like and other protein of small size (EKC⁄KEOPS) complex, known to be involved in the control of transcription and telomere homeo-stasis. | ỊFEBS Journal Phosphorylation of the Saccharomyces cerevisiae Grx4p glutaredoxin by the Bud32p kinase unveils a novel signaling pathway involving Sch9p a yeast member of the Akt PKB subfamily Caterina Peggion1 Raffaele Lopreiato1 Elena Casanova1 Maria Ruzzene1 2 Sonia Facchin1 Lorenzo A. Pinna1 2 Giovanna Carignani1 and Geppo Sartori1 1 Dipartimento di Chimica Biologica dell Universitej di Padova Italy 2 Venetian Institute of Molecular Medicine VIMM Padova Italy Keywords Bud32p kinase EKC KEOPS complex Grx4p glutaredoxin Sch9p kinase Correspondence G. Sartori Dipartimento di Chimica Biologica dell Universita di Padova viale G. Colombo 3-35121 Padova Italy Fax 39 049 80733I0 Tel 39 049 8276141 E-mail These authors contributed equally to this work Received 31 July 2008 revised 26 September 2008 accepted 1 October 2008 doi The Saccharomyces cerevisiae atypical protein kinase Bud32p is a member of the nuclear endopeptidase-like kinase chromatin-associated kinase endopeptidase-like and other protein of small size EKC KEOPS complex known to be involved in the control of transcription and telomere homeostasis. Complex subunits Pcc1p Pcc2p Cgi121p Kae1p represent however a small subset of the proteins able to interact with Bud32p suggesting that this protein may be endowed with additional roles unrelated to its participation in the EKC KEOPS complex. In this context we investigated the relationships between Bud32p and the nuclear glutaredoxin Grx4p showing that it is actually a physiological substrate of the kinase and that Bud32p contributes to the full functionality of Grx4p in vivo. We also show that this regulatory system is influenced by the phosphorylation of Bud32p at Ser258 which is specifically mediated by the Sch9p kinase yeast homolog of mammalian protein kinase B Akt PKB . Notably Ser258 phosphorylation of Bud32p does not alter the catalytic activity of the protein kinase per se but positively regulates .

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