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CDH1 binds MAD2L2 in a Rev1-like pattern.

Nomi Pernicone1, Shira Grinshpon1, Tamar Listovsky2

  • 1Department of Molecular Biology, Ariel University, Ariel, Israel.

Biochemical and Biophysical Research Communications
|August 20, 2020
PubMed
Summary
This summary is machine-generated.

MAD2L2 protein

Keywords:
CDH1(FZR1)MAD2L2Protein-protein interaction

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • MAD2L2 (Rev7) is a key regulator in DNA repair, translesion synthesis (TLS), and mitosis.
  • It forms complexes with proteins like Rev3 (Pol ζ) and is part of the shieldin complex.
  • MAD2L2 also inhibits premature anaphase by binding CDH1.

Purpose of the Study:

  • To elucidate the molecular mechanisms of MAD2L2's interaction with CDH1 and its homodimerization.
  • To investigate the structural basis for MAD2L2's binding preferences in different complexes.

Main Methods:

  • Utilized a series of MAD2L2 mutants in a human cell line.
  • Analyzed protein-protein interactions (PPIs) to determine binding interfaces.

Main Results:

  • The C-terminus of MAD2L2 is crucial for both CDH1 binding and MAD2L2 homodimerization.
  • CDH1 binds MAD2L2 using the same C-terminal residues that Rev1 interacts with.
  • This suggests a conserved binding motif for Rev1-like proteins on MAD2L2.

Conclusions:

  • MAD2L2's C-terminus mediates interactions with CDH1 and facilitates homodimerization.
  • CDH1 acts as an additional Rev1-like binding partner for MAD2L2.
  • These findings highlight MAD2L2's versatility and the intricate regulation of its complex formation.