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AMP-activated protein kinase adapts rRNA synthesis to cellular energy supply
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Journal Article
AMP-activated protein kinase adapts rRNA synthesis to cellular energy supply
2009
Overview
AMP-activated protein kinase (AMPK) senses changes in the intracellular AMP/ATP ratio, switching off energy-consuming processes and switching on catabolic pathways in response to energy depletion. Here, we show that AMPK down-regulates rRNA synthesis under glucose restriction by phosphorylating the RNA polymerase I (Pol I)-associated transcription factor TIF-IA at a single serine residue (Ser-635). Phosphorylation by AMPK impairs the interaction of TIF-IA with the TBP-containing promoter selectivity factor SL1, thereby precluding the assembly of functional transcription initiation complexes. Mutation of Ser-635 compromises down-regulation of Pol I transcription in response to low energy supply, supporting that activation of AMPK adapts rRNA synthesis to nutrient availability and the cellular energy status.
Publisher
National Academy of Sciences,National Acad Sciences
Subject
/ Adenosine Triphosphate - metabolism
/ AMP-activated protein kinase
/ AMP-Activated Protein Kinases - metabolism
/ Animals
/ Cells
/ Energy
/ Glucose
/ Humans
/ Kinases
/ Mice
/ Mutation
/ Pol1 Transcription Initiation Complex Proteins - antagonists & inhibitors
/ Pol1 Transcription Initiation Complex Proteins - chemistry
/ Pol1 Transcription Initiation Complex Proteins - genetics
/ Pol1 Transcription Initiation Complex Proteins - metabolism
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ RNA
/ RNA Polymerase I - metabolism
/ RNA, Ribosomal - biosynthesis
/ serine
