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Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications
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Published on: April 21, 2023

New insights into Dok-4 PTB domain structure and function.

Erika Hooker1, Cindy Baldwin, Serge Lemay

  • 1Department of Medicine, Division of Nephrology, McGill University Health Centre, Montreal, Quebec, Canada H3A 2B4.

Biochemical and Biophysical Research Communications
|September 18, 2012
PubMed
Summary

Dok-4 adapter protein binding to Ret requires extended PTB domain elements. This interaction is crucial for Dok-4

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Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
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Area of Science:

  • Molecular biology
  • Cell signaling
  • Immunology

Background:

  • Dok adapter proteins regulate immune cell signaling via their conserved phosphotyrosine-binding (PTB) domains.
  • Dok-1, -2, and -3 interact with Ship1, a phosphatase involved in inhibitory signaling.
  • Dok-4 is widely expressed but its function is poorly understood due to limited knowledge of its binding partners.

Purpose of the Study:

  • To elucidate the structural and functional basis of Dok-4's interaction with its binding partners.
  • To define the precise boundaries of the Dok-4 PTB domain required for Ret binding.
  • To investigate the role of Dok-4 in inhibitory signaling pathways.

Main Methods:

  • Co-immunoprecipitation assays to study protein-protein interactions.
  • Analysis of Dok-4 PTB domain mutants for binding to Ret and Ship1.
  • Investigation of a human single nucleotide polymorphism (SNP) in Dok-4.

Main Results:

  • Dok-4 binding to Ret requires C-terminal residues beyond the canonical PTB domain, extending into an alpha-helix.
  • The Dok-4 PTB domain binds phosphorylated NPXY motifs in Ship1, but not Ship2.
  • A human R186H SNP in the Dok-4 PTB domain abolishes Ret-mediated tyrosine phosphorylation.

Conclusions:

  • The Dok-4 PTB domain has extended structural elements crucial for Ret binding.
  • Dok-4 interacts with Ship1, suggesting a role in inhibitory signaling in T-cells.
  • A Dok-4 R186H polymorphism may lead to a rare Dok-4-related human phenotype.