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ProteomicsInterrogating the interaction of fission yeast RNA-binding protein Puf3 with the Ccr4-Not complex using crosslinking mass spectrometry
mRNA decay is a key determinant of gene regulation, initiated by the shortening of mRNA poly(A) tails by the CCR4-NOT deadenylation complex. Specificity is achieved through RNA adaptors—RNA-binding proteins that recruit CCR4-NOT to specific substrate mRNAs in a regulated manner. However, the molecul...
ORGANISM(S): Schizosaccharomyces pombe 927 
2025-09-03 | PXD055147 | Pride
Crosslinking ms Idr Protein-protein interaction Rna binding protein puf3 Ccr4-not complex 
ProteomicsIdentification of acetylation-regulated interactors of the human CCR4-NOT complex
The evolutionarily conserved CCR4-NOT complex acts as a central player in the control of mRNA turnover and mediates accelerated mRNA degradation upon histone deacetylase (HDAC) inhibition. Here, we explored acetylation-induced changes in the composition of the CCR4-NOT complex by purification of the...
ORGANISM(S): Homo sapiens (Human) 
2021-12-15 | PXD027237 | Pride
Rnf219 Mrna turnover Protein acetylation Deadenylation E3 ubiquitin ligase Ccr4-not complex 
TranscriptomicsSpecific Roles for the Ccr4-Not Complex Subunits in Expression of the Genome
These Affymetrix data were used to determine the role of each non-essential subunit of the conserved Ccr4-Not complex in the control of gene expression in the yeast S. cerevisiae. The study was performed with cells growing exponentially in high glucose and with cells grown to glucose depletion. Spec...
ORGANISM(S): Saccharomyces cerevisiae 
2008-12-10 | E-GEOD-10521 | biostudies-arrayexpress
ProteomicsCcr4-Not ubiquitin ligase signaling regulates ribosomal protein homeostasis and inhibits 40S ribosomal autophagy
The Ccr4-Not complex containing the Not4 ubiquitin ligase regulates gene transcription and mRNA decay, yet it also has poorly defined roles in translation, proteostasis, and endolysosomal-dependent nutrient signaling. To define how Ccr4-Not mediated ubiquitin signaling regulates these additional pro...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-10-17 | PXD044420 | Pride
Autophagy Endolysomal Ribosome Ccr4-not Not4 
GenomicsThe CCR4-NOT complex suppresses untimely translational activation of maternal mRNAs.
The CCR4-NOT complex suppresses untimely translational activation of maternal mRNAs.
PRJNA930503 | ENA
TranscriptomicsTranscription profiling of S. cerevisiae wild type reference strain, two simple mutants (not1-2 and spt3) and one double mutant (not1-2 spt3) reveals a SAGA-Independent function of SPT3 mediates transcriptional deregulation in a mutant of the Ccr4-Not Complex
The conserved multi-subunit Ccr4-Not complex regulates gene expression in diverse ways. In this work, we characterize the suppression of temperature sensitivity associated with a mutation in the gene encoding the scaffold subunit of the Ccr4-Not complex, NOT1, by the deletion of SPT3. We determine t...
ORGANISM(S): Saccharomyces cerevisiae 
2008-06-16 | E-GEOD-9432 | biostudies-arrayexpress
ProteomicsInsulin-degrading enzyme regulates mRNA processing and in-teracts with the CCR4-NOT transcription complex
Insulin-degrading enzyme is zinc metallo protease degrading low molecular weight substrates including insulin. Ubiquitous expression, high evolutionary conservation, upregulation of Ide in stress situations, and various literature findings suggest a broader function of Ide in cell physiology and pro...
ORGANISM(S): Homo sapiens (Human) 
2025-06-16 | PXD060228 | Pride
Insulinase  protein homeostasis  rna processing  ccr4-not  beta cell  islet of langerhans Timstof pro 
GenomicsThe Ccr4-Not complex monitors the translating ribosome for codon optimality
The Ccr4-Not complex monitors the translating ribosome for codon optimality
PRJNA543493 | ENA
GenomicsThe Ccr4-Not complex monitors the translating ribosome for codon optimality
The Ccr4-Not complex monitors the translating ribosome for codon optimality
PRJNA603124 | ENA
ProteomicsCharacterization of BioID tagging systems in budding yeast and exploring the interactome of the Ccr4-Not complex
The modified E. coli biotin ligase BirA* was the first developed for proximity labeling of proteins (BioID). However, it has low activity at temperatures below 37 C, which reduces its effectiveness in organisms growing at lower temperatures, such as budding yeast. Multiple derivatives of the enzymes...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2024-05-02 | MSV000094663 | MassIVE
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