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Actin filaments undergo polymerization and depolymerization from either end. The polymerization and depolymerization rates depend on the cytosolic concentration of free G-actins. The polymerization rate is generally higher at the plus or barbed end, while the depolymerization rate is higher at the minus or pointed end. At a steady state, critical concentration describes the concentration of free G-actin monomers at which the polymerization rate at the plus end is equal to that of the...
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Related Experiment Video

Updated: Oct 7, 2025

RBDT: A Computerized Task System based in Transposition for the Continuous Analysis of Relational Behavior Dynamics in Humans
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TAT-RHIM: a more complex issue than expected.

Benedikt Kolbrink1, Theresa Riebeling1, Nikolas K Teiwes2

  • 1Department of Nephrology and Hypertension, University Hospital Schleswig-Holstein, 24105 Kiel, Germany.

The Biochemical Journal
|January 11, 2022
PubMed
Summary
This summary is machine-generated.

Murine cytomegalovirus protein M45

Keywords:
M45RHIM domaincell deathprotein transduction

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Area of Science:

  • Virology
  • Cell Biology
  • Immunology

Background:

  • Murine cytomegalovirus protein M45 possesses a RIP homotypic interaction motif (RHIM) that inhibits necroptotic cell death.
  • RHIM domains are crucial in inflammatory signaling and regulated cell death (RCD) pathways.
  • Regulated necrosis contributes to tissue damage in various diseases.

Purpose of the Study:

  • To develop a therapeutic agent harnessing M45's cell death-suppressive properties.
  • To investigate the potential of a synthetic peptide derived from M45's RHIM domain.

Main Methods:

  • A synthetic peptide containing the M45 RHIM domain was created.
  • The peptide was fused with a protein transduction domain for cellular delivery.
  • The peptide's effect on various cell lines, including cancer cells, was evaluated.

Main Results:

  • The engineered peptide efficiently entered eukaryotic cells.
  • Unexpectedly, the peptide induced necrosis-like cell death in all tested cancer and primary cells.
  • This novel cell death mechanism was resistant to known RCD inhibitors and involved biomembrane disruption.

Conclusions:

  • A synthetic M45 RHIM peptide, delivered via a transduction domain, induces a unique necrotic cell death.
  • This novel cell death induction mechanism shows potential for targeting resistant cancer cells.
  • Findings suggest a new therapeutic strategy for combating challenging malignancies.