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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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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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Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
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Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
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Identification of EGFR and RAS Inhibitors using Caenorhabditis elegans
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Inhibition of Ras signaling by blocking Ras-effector interactions with cyclic peptides.

Punit Upadhyaya1, Ziqing Qian1, Nicholas G Selner1

  • 1Department of Chemistry and Biochemistry, The Ohio State University, 484 West 12th Avenue, Columbus, OH 43210 (USA).

Angewandte Chemie (International Ed. in English)
|May 8, 2015
PubMed
Summary
This summary is machine-generated.

Researchers developed cell-permeable cyclic peptides to target mutant Ras proteins, a significant challenge in cancer therapy. These novel peptides inhibit Ras signaling, block protein interactions, and induce cancer cell death, offering a new therapeutic strategy.

Keywords:
Ras signalingcancercell-penetrating peptidescyclic peptidesprotein-protein interactions

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Area of Science:

  • Oncology
  • Molecular Biology
  • Drug Discovery

Background:

  • Ras genes are frequently activated in human cancers.
  • Mutant Ras proteins are considered
  • undruggable
  • due to a lack of accessible binding pockets.

Purpose of the Study:

  • To discover novel inhibitors targeting mutant Ras proteins.
  • To develop cell-permeable cyclic peptides for cancer therapy.
  • To explore the potential of inhibiting intracellular protein-protein interactions.

Main Methods:

  • Screening of a combinatorial peptide library.
  • Structure-activity relationship (SAR) analysis.
  • Assessment of Ras-binding and cell-penetrating properties of cyclic peptides.

Main Results:

  • Discovery of a family of cyclic peptides with Ras-binding and cell-penetrating capabilities.
  • Demonstration that these peptides inhibit Ras signaling by binding to Ras-GTP.
  • Confirmation of blocked Ras-GTP interaction with downstream proteins.
  • Induction of apoptosis in cancer cells by the cyclic peptides.

Conclusions:

  • Cyclic peptides can be developed to inhibit intracellular protein-protein interactions.
  • These findings present a novel class of direct Ras inhibitors as potential anticancer agents.