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Weiss EL Kurischko C Zhang C Shokat K Drubin DG Luca FC 《The Journal of cell biology》2002,158(5):885-900
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Diana M. Calderón-Nore?a Alberto González-Novo Sara Orellana-Mu?oz Pilar Gutiérrez-Escribano Yolanda Arnáiz-Pita Encarnación Due?as-Santero M. Belén Suárez Marie-Elisabeth Bougnoux Francisco del Rey Gavin Sherlock Christophe d’Enfert Jaime Correa-Bordes Carlos R. Vázquez de Aldana 《PLoS genetics》2015,11(4)
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Cristina Panozzo Myriam Bourens Aleksandra Nowacka Christopher James Herbert 《Molecular genetics and genomics : MGG》2010,283(2):111-122
In Saccharomyces cerevisiae, the RAM network is involved in cell separation after cytokinesis, cell integrity and cell polarity. The key function of
this network is the regulation of the activity of the protein kinase Cbk1p, which is a member of the conserved NDR kinase
family. Cbk1p function is controlled by its sub-cellular localization and at least two phosphorylation events: an auto phosphorylation
in the kinase domain (S570) and the phosphorylation of a C-terminal hydrophobic motif by an upstream kinase (T743). After
a UV mutagenesis, we have isolated 115 independent extragenic suppressors of four ∆ram mutations: ∆tao3, ∆hym1, ∆kic1 and ∆sog2. Over 50% of the suppressors affect a single residue in Cbk1p (S745F), which is close to the phosphorylation site in the
hydrophobic motif. Our results show that the CBK1-S745F allele leads to a constitutively active form of Cbk1p that is independent of the upstream RAM network. We hypothesize that
the mutant Cbk1-S745Fp mimics the effect of the phosphorylation of T743. 相似文献