Genomes and Genes
Martine A Collart
Affiliation: University of Geneva
- Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29Olesya O Panasenko
Department of Microbiology and Molecular Medicine, University of Geneva, Faculty of Medicine, Geneva, Switzerland
Mol Cell Biol 31:1610-23. 2011..In the absence of Not4, Ecm29 interacts less well with the proteasome and becomes ubiquitinated and degraded. Our results characterize Ecm29 as a proteasome chaperone whose appropriate interaction with the proteasome requires Not4...
- The Not3/5 subunit of the Ccr4-Not complex: a central regulator of gene expression that integrates signals between the cytoplasm and the nucleus in eukaryotic cellsMartine A Collart
Dpt of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, 1 rue Michel Servet, 1211 Geneve 4, Switzerland
Cell Signal 25:743-51. 2013..This review will summarize recent evidence designing the Not3/5 module of the Ccr4-Not complex as a functional module involved in coordination of the regulation of gene expression between the nucleus and the cytoplasm...
- The Ccr4--not complexMartine A Collart
Dpt Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, 1 rue Michel Servet, 1211 Geneva 4, Switzerland
Gene 492:42-53. 2012..Finally, based upon our current state of knowledge, we will propose a model to explain how one complex can provide such multi-functionality. This model suggests that the Ccr4-Not complex might function as a "chaperone platform"...
- Specific roles for the Ccr4-Not complex subunits in expression of the genomeNowel Azzouz
Department of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Geneva 4, Switzerland
RNA 15:377-83. 2009..From the study of only two different growth conditions, revealing an impact of the Ccr4-Not complex on more than 85% of all studied genes, we can infer that the Ccr4-Not complex is important for expression of most of the yeast genome...
- The Ccr4-not complex regulates Skn7 through Srb10 kinaseEve Lenssen
Department of Microbiology and Molecular Medicine, University of Geneva Medical School, CMU, 1 rue Michel Servet, 1211 Geneva 4, Switzerland
Eukaryot Cell 6:2251-9. 2007..These results reveal a critical role for the Ccr4-Not complex in the mechanism of activation of Skn7 that is dependent upon the Srb10 kinase...
- The Ccr4-Not complex independently controls both Msn2-dependent transcriptional activation--via a newly identified Glc7/Bud14 type I protein phosphatase module--and TFIID promoter distributionEve Lenssen
Département de Microbiologie et Médecine Moléculaire, CMU, 1 rue Michel Servet, 1211 Geneva 4, Switzerland
Mol Cell Biol 25:488-98. 2005..Thus, increased activity of STRE genes in ccr4-not mutants may result from both altered general distribution of TFIID and unscheduled activation of Msn2...
- The yeast Ccr4-Not complex controls ubiquitination of the nascent-associated polypeptide (NAC-EGD) complexOlesya Panasenko
Department of Microbiology and Molecular Medicine, University of Geneva Medical School, 1211 Geneva 4, Switzerland
J Biol Chem 281:31389-98. 2006..Taken together our results reveal that the EGD ribosome-associated complex is ubiquitinated in a regulated manner, and they show a new role for the Ccr4-Not complex in this ubiquitination...
- The Ccr4-not complex and yTAF1 (yTaf(II)130p/yTaf(II)145p) show physical and functional interactionsCécile Deluen
Departement de Biochimie Medicale, CMU, 1211 Geneva 4, Switzerland
Mol Cell Biol 22:6735-49. 2002....
- The CCR4-NOT complex physically and functionally interacts with TRAMP and the nuclear exosomeNowel Azzouz
Department of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland
PLoS ONE 4:e6760. 2009..However, there has been no evidence so far that this complex is important for RNA degradation in the nucleus...
- Ribosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitinationOlesya O Panasenko
Swiss Institute for Bioinformatics, University of Geneva, 1211 Geneva 4, Switzerland
Genetics 181:447-60. 2009..Finally, our study demonstrated an interaction of EGD/NAC with the proteasome and revealed the importance of the Not4p E3 ligase, responsible for EGD/NAC ubiquitination, in this association...
- Presence of Not5 and ubiquitinated Rps7A in polysome fractions depends upon the Not4 E3 ligaseOlesya O Panasenko
Department of Microbiology and Molecular Medicine, University of Geneva, Faculty of Medicine, 1 rue Michel Servet, 1211 Geneva 4, Switzerland
Mol Microbiol 83:640-53. 2012..These results lead us to suggest that Not4 contributes to normal polysome levels and is important for cellular protein solubility maybe in part by ubiquitination of Rps7A...
- The eukaryotic Ccr4-not complex: a regulatory platform integrating mRNA metabolism with cellular signaling pathways?Martine A Collart
Department of Medical Biochemistry, CMU, 1 rue Michel Servet, 1211 Geneva 4, Switzerland
Prog Nucleic Acid Res Mol Biol 77:289-322. 2004
- LKB1 interacts with and phosphorylates PTEN: a functional link between two proteins involved in cancer predisposing syndromesHamid Mehenni
Departement de Biologie Cellulaire, Universite de Geneve, 1211 Geneve 4, Switzerland
Hum Mol Genet 14:2209-19. 2005....
- Interaction between Not1p, a component of the Ccr4-not complex, a global regulator of transcription, and Dhh1p, a putative RNA helicaseLaurent Maillet
Department of Medical Biochemistry, University of Geneva Medical School, 1 rue Michel Servet, 1211 Geneva 4, Switzerland
J Biol Chem 277:2835-42. 2002....
- The Not4 E3 Ligase and CCR4 Deadenylase Play Distinct Roles in Protein Quality ControlDavid Halter
Department of Microbiology and Molecular Medicine, Faculty of Medicine, Institute of Genetics and Genomics of Geneva, University of Geneva, Geneva, Switzerland
PLoS ONE 9:e86218. 2014..We concluded that Not4 plays a role in protein quality control independently of the Ccr4 deadenylase, and that it is involved in clearance of aberrant proteins at least in part via the proteasome. ..