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B Cell Receptor Activation Predominantly Regulates AKT-mTORC1/2 Substrates Functionally Related to RNA Processing.

Dara K Mohammad1,2, Raja H Ali3, Janne J Turunen1

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Researchers identified novel protein phosphorylation events regulated by Protein kinase B (AKT) and mTORC1/2 signaling following B cell receptor activation. This revealed conserved protein targets involved in gene regulation and RNA processing.

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Area of Science:

  • Cellular signaling pathways
  • Molecular biology
  • Proteomics

Background:

  • Protein kinase B (AKT) phosphorylates substrates at the RXRXXpS/T motif, facilitating 14-3-3 interactions.
  • B cell receptor (BCR) activation triggers complex signaling cascades impacting cellular functions.

Purpose of the Study:

  • To identify novel AKT-induced phosphorylation events after BCR activation.
  • To characterize proteins regulated by this signaling pathway.

Main Methods:

  • Proteomics, including phosphorylated consensus motif-specific antibody enrichment and tandem mass spectrometry.
  • Biochemical assays and bioinformatics analyses.
  • Inhibition studies using AKT (MK-2206) and mTORC (PP242) inhibitors.

Main Results:

  • Identified 446 proteins with 186 novel phosphorylation events.
  • Observed differential regulation: 85 proteins upregulated (ribosomal, translational, DNA/transcription regulation) and 277 downregulated (RNA binding, splicing, export).
  • Confirmed RXRXXpS/T motif as a substrate for both AKT and mTORC1/2, with domain-specific enrichment and phylogenetic conservation.

Conclusions:

  • BCR activation induces widespread phosphorylation changes mediated by AKT and mTORC1/2.
  • The RXRXXpS/T motif is a key regulatory site for conserved protein functions across eukaryotes.
  • Phosphorylation dynamics impact gene expression and RNA processing machinery.