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Ras-related nuclear protein or Ran is a small G protein that cycles between its GTP and GDP bound states. Ran specific regulators, a Ran GTPase Activating Protein or RanGAP present in the cytosol and a Ran guanine nucleotide exchange factor or RanGEF present inside the nucleus regulate GTP/GDP exchange. A high concentration of GTP inside the cells, in addition to this asymmetric distribution of  Ran-specific regulators, leads to a higher RanGTP concentration inside the nucleus. This...
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Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
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Isolation of CA1 Nuclear Enriched Fractions from Hippocampal Slices to Study Activity-dependent Nuclear Import of Synapto-nuclear Messenger Proteins
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RAM function is dependent on Kapβ2-mediated nuclear entry.

Thomas Gonatopoulos-Pournatzis1, Victoria H Cowling1

  • 1*MRC Protein Phosphorylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.

The Biochemical Journal
|November 9, 2013
PubMed
Summary
This summary is machine-generated.

The RNMT-activating mini-protein (RAM) subunit is essential for RNA guanine-7 methyltransferase (RNMT) activity in eukaryotic gene expression. This study identifies the specific RAM domain responsible for RNMT activation and nuclear import.

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Area of Science:

  • Molecular Biology
  • Gene Expression Regulation
  • Biochemistry

Background:

  • Eukaryotic gene expression relies on 7-methylguanosine cap addition to pre-mRNA.
  • This cap structure protects RNA and facilitates transcription, processing, and translation.
  • Cap synthesis involves RNA guanylyltransferase and 5'-phosphatase (RNGTT) and RNA guanine-7 methyltransferase (RNMT).

Purpose of the Study:

  • To investigate the interaction between RNMT and its activating subunit, RAM (RNMT-activating mini-protein).
  • To identify the specific domain of RAM responsible for RNMT activation and stabilization.
  • To elucidate the mechanism of RAM's nuclear import.

Main Methods:

  • Protein interaction studies to map the RNMT-binding domain of RAM.
  • Analysis of RAM domain fragments for RNMT activation and stabilization.
  • Investigation of nuclear localization signals and karyopherin-mediated transport for RAM.

Main Results:

  • The N-terminal 45 amino acids of RAM are necessary and sufficient for maximal RNMT activation.
  • Smaller regions of this RAM domain are sufficient for RNMT stabilization.
  • RAM's nuclear import is mediated by PY nuclear localization signals and Kapβ2.

Conclusions:

  • RAM plays a critical role in cellular cap methylation and cell viability by activating and stabilizing RNMT.
  • Specific domains within RAM dictate its function in RNMT activation versus stabilization.
  • RAM is imported into the nucleus via a defined transport pathway involving Kapβ2.