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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

BUD32 Bud32p

Bud32, PRPK, piD261, p53-related protein kinase, Bud32p
Top mentioned proteins: p53, CAN, ATPase, Inactive, Akt
Papers on Bud32
The Levels of a Universally Conserved tRNA Modification Regulate Cell Growth.
New
Glavic et al., Santiago, Chile. In J Biol Chem, Aug 2015
Yeast lacking central components of the t(6)A synthesis machinery, such as Tcs3p (Kae1p) or Tcs5p (Bud32p), show slow-growth phenotypes.
Crystal structures of the Gon7/Pcc1 and Bud32/Cgi121 complexes provide a model for the complete yeast KEOPS complex.
New
van Tilbeurgh et al., Orsay, France. In Nucleic Acids Res, May 2015
The yeast KEOPS protein complex comprising Kae1, Bud32, Cgi121, Pcc1 and Gon7 is responsible for the essential tRNA threonylcarbamoyladenosine (t(6)A) modification.
Kinase-associated endopeptidase 1 (Kae1) participates in an atypical ribosome-associated complex in the apicoplast of Plasmodium falciparum.
Goldberg et al., Saint Louis, United States. In J Biol Chem, 2014
Our results show that cytoplasmic Kae1 forms a complex with Bud32 and Cgi121 as in other organisms, whereas apicoplast Kae1 makes novel interactions with multiple proteins in the apicoplast.
NleH defines a new family of bacterial effector kinases.
Cygler et al., Saskatoon, Canada. In Structure, 2014
NleHs and their homologous effector kinases form a new kinase family within the cluster of eukaryotic-like kinases that includes also Rio, Bud32, and KdoK families.
Functional assignment of KEOPS/EKC complex subunits in the biosynthesis of the universal t6A tRNA modification.
Basta et al., Vandœuvre-lès-Nancy, France. In Nucleic Acids Res, 2013
The KEOPS/EKC complex is composed of Kae1, a universal metalloprotein belonging to the ASHKA superfamily of ATPases; Bud32, an atypical protein kinase and two small proteins, Cgi121 and Pcc1.
Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system.
Sicheri et al., Toronto, Canada. In Nucleic Acids Res, 2013
In bacteria, YgjD orthologues operate in concert with the bacterial-specific proteins YeaZ and YjeE, whereas in archaeal and eukaryotic systems, Kae1 operates as part of a larger macromolecular assembly called KEOPS with Bud32, Cgi121, Gon7 and Pcc1 subunits.
The Drosophila EKC/KEOPS complex: roles in protein synthesis homeostasis and animal growth.
Glavic et al., Santiago, Chile. In Fly (austin), 2013
We recently identified the Bud32 (yeast)/PRPK (human) ortholog in Drosophila, Prpk (p53-related protein kinase), and found that it is required for TOR kinase activity.
Drosophila p53-related protein kinase is required for PI3K/TOR pathway-dependent growth.
Glavic et al., Santiago, Chile. In Development, 2013
p53-related protein kinase (Bud32/PRPK) has been identified as a protein involved in proliferation through its effects on transcription in yeast and p53 stabilization in human cell culture.
Evidence that two Pcl-like cyclins control Cdk9 activity during cell differentiation in Aspergillus nidulans asexual development.
Fischer et al., Karlsruhe, Germany. In Eukaryot Cell, 2013
Using yeast two-hybrid screens, we identified a third cyclin, PclB, and a kinase, PipA(Bud32).
Mechanism-based screen establishes signalling framework for DNA damage-associated G1 checkpoint response.
Mittnacht et al., London, United Kingdom. In Plos One, 2011
Instead our results predict signalling involving the known TP53 phosphorylating kinase PRPK/TP53RK and the JNK/p38MAPK activating kinase STK4/MST1, both hitherto unrecognised for their contribution to DNA damage G1 checkpoint signalling.
Cell polarity in Saccharomyces cerevisiae depends on proper localization of the Bud9 landmark protein by the EKC/KEOPS complex.
GeneRIF
Hirano et al., Yokohama, Japan. In Genetics, 2011
EKC/KEOPS complex is specifically involved in the regulation of Bud9p localization downstream of Rax1p/Rax2p.
The activity of an ancient atypical protein kinase is stimulated by ADP-ribose in vitro.
Kennelly et al., Blacksburg, United States. In Arch Biochem Biophys, 2011
Despite the fact that phylogenetic analyses indicate that the piD261/Bud32 protein kinases descend directly from the primordial ancestor of the "eukaryotic" protein kinase superfamily, our knowledge of their physiological role is relatively fragmentary and largely limited to two eucaryal representatives: piD261/Bud32 from yeast and the p53-related protein kinase from humans.
The highly conserved KEOPS/EKC complex is essential for a universal tRNA modification, t6A.
Sternglanz et al., Stony Brook, United States. In Embo J, 2011
The complex consists of five proteins, Kinase-Associated Endopeptidase (Kae1), a highly conserved protein present in bacteria, archaea and eukaryotes, a kinase (Bud32) and three additional small polypeptides.
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.
GeneRIF
Sartori et al., Padova, Italy. In Febs J, 2008
Sch9 phosphorylates, both in vitro and in vivo, Ser258 of Bud32. This modification does not affect the catalytic properties of Bud32, but promotes its ability to associate with its substrate Grx4p and, consequently, to phosphorylate it.
Structure of the archaeal Kae1/Bud32 fusion protein MJ1130: a model for the eukaryotic EKC/KEOPS subcomplex.
van Tilbeurgh et al., Orsay, France. In Embo J, 2008
The Bud32p and kinase-associated endopeptidase 1 (Kaelp) components of the complex are totally conserved in eukarya and archaea.
Phosphorylation and activation of the atypical kinase p53-related protein kinase (PRPK) by Akt/PKB.
GeneRIF
Pinna et al., Padova, Italy. In Cell Mol Life Sci, 2007
activation of PRPK is mediated by another kinase, Akt/PKB, which phosphorylates PRPK at Ser250
A Small Ras-like protein Ray/Rab1c modulates the p53-regulating activity of PRPK.
GeneRIF
Kito et al., Japan. In Biochem Biophys Res Commun, 2006
A Small Ras-like GTPase protein Ray was indicated to modulate p53 transcriptional activity of PRPK.
A genome-wide screen identifies the evolutionarily conserved KEOPS complex as a telomere regulator.
Impact
Durocher et al., Toronto, Canada. In Cell, 2006
Cgi121 is part of a conserved protein complex -- the KEOPS complex -- containing the protein kinase Bud32, the putative peptidase Kae1, and the uncharacterized protein Gon7.
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