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Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
Phosphorylation01:02

Phosphorylation

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A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3
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A High Resolution Method to Monitor Phosphorylation-dependent Activation of IRF3

Published on: January 24, 2016

Phosphorylation regulates human T-cell leukemia virus type 1 Rex function.

Matthew Kesic1, Rami Doueiri, Michael Ward

  • 1Center for Retrovirus Research, The Ohio State University, Columbus, OH 43210, USA. kesic.1@osu.edu

Retrovirology
|November 19, 2009
PubMed
Summary
This summary is machine-generated.

Researchers mapped phosphorylation sites on Human T-cell leukemia virus type 1 Rex protein (Rex-1). Phosphorylation at Ser-97 and Thr-174 is critical for Rex-1 function, offering insights into viral regulation.

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Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants
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Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants

Published on: June 6, 2025

Area of Science:

  • Virology
  • Molecular Biology
  • Protein Biochemistry

Background:

  • Human T-cell leukemia virus type 1 (HTLV-1) causes ATL and HAM/TSP.
  • HTLV-1 encodes regulatory proteins Tax and Rex, crucial for viral replication and cell transformation.
  • Rex-1, a phosphoprotein, regulates viral mRNA export and its function is potentially modulated by phosphorylation.

Purpose of the Study:

  • To perform a comprehensive phosphorylation analysis of HTLV-1 Rex-1.
  • To identify specific phosphorylation sites on Rex-1.
  • To determine the functional significance of identified phosphorylation sites.

Main Methods:

  • Overexpression of Rex-1 in 293 T cells.
  • Phosphorylation mapping using affinity purification and liquid chromatography tandem mass spectrometry.
  • Site-directed mutational analysis and Rex reporter assays to assess functional significance.

Main Results:

  • Achieved 100% physical coverage of the Rex-1 polypeptide.
  • Identified five novel phosphorylation sites: Thr-22, Ser-36, Thr-37, Ser-97, and Ser-106.
  • Confirmed phosphorylation at Ser-70 and Thr-174, and found it critical for Rex-1 function. No phosphorylation at Ser-177.

Conclusions:

  • Completely mapped site-specific phosphorylation of Rex-1, identifying seven residues.
  • This study is the first to fully map Rex-1 phosphorylation sites.
  • Provides critical insights into the regulatory mechanisms governing Rex-1 function.