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Related Experiment Videos

Physical and functional interaction between hMSH5 and c-Abl.

Wei Yi1, Tai-Hsien Lee, Joshua D Tompkins

  • 1School of Molecular Biosciences and Center for Reproductive Biology, Washington State University, Pullman, Washington 99164-4660, USA.

Cancer Research
|January 7, 2006
PubMed
Summary

Human MutS homolog 5 (hMSH5) interacts with c-Abl tyrosine kinase, influencing DNA damage response. This interaction activates c-Abl and affects hMSH5 phosphorylation and complex formation, impacting cellular responses to radiation.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • The biological roles of human MutS homolog 5 (hMSH5) in human cells remain largely unknown.
  • c-Abl is a key non-receptor tyrosine kinase involved in cellular functions, including DNA damage response, typically suppressed without cellular stress.

Purpose of the Study:

  • To investigate the potential physical and functional interaction between hMSH5 and c-Abl.
  • To elucidate the role of this interaction in cellular responses to DNA damage, particularly ionizing radiation.

Main Methods:

  • In vivo co-immunoprecipitation assays to detect protein-protein interactions.
  • Analysis of protein domains involved in the interaction.
  • Assessment of c-Abl kinase activity and hMSH5 phosphorylation.

Related Experiment Videos

  • Investigation of hMSH4-hMSH5 heterocomplex stability.

    • Main Results:

    • hMSH5 physically interacts with c-Abl in vivo via its NH2 terminus and the c-Abl SH3 domain.
    • This interaction activates c-Abl tyrosine kinase and leads to hMSH5 phosphorylation upon ionizing radiation exposure.
    • A specific variant, hMSH5 P29S, overactivates c-Abl tyrosine kinase.
    • Tyrosine phosphorylation of hMSH5 promotes the dissociation of the hMSH4-hMSH5 heterocomplex.

    Conclusions:

    • A novel physical and functional link between hMSH5 and c-Abl has been identified.
    • The interplay between hMSH5 and c-Abl modulates cellular responses to ionizing radiation-induced DNA damage.
    • This interaction provides new insights into DNA repair mechanisms and the regulation of c-Abl activity.