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Related Experiment Videos

Kinase activation through dimerization by human SH2-B.

Masahiro Nishi1, Eric D Werner, Byung-Chul Oh

  • 1Joslin Diabetes Center, One Joslin Place, Boston, MA 02215, USA.

Molecular and Cellular Biology
|March 16, 2005
PubMed
Summary
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SH2-B and APS proteins homodimerize and heterodimerize, modulating JAK2 kinase activity. This dimerization controls cytokine and growth factor signaling, acting as both an activator and inhibitor.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Protein Interactions

Background:

  • SH2-B, APS, and Lnk are signaling protein family members.
  • These proteins can activate, mediate, or inhibit cytokine and growth factor signaling pathways.

Purpose of the Study:

  • To investigate the homodimerization and heterodimerization of SH2-B and APS isoforms.
  • To elucidate the role of these dimerization events in JAK2 kinase activation and signaling modulation.

Main Methods:

  • Yeast two-hybrid assays
  • Cellular transfection assays
  • Analysis of protein-protein interactions and kinase activity

Main Results:

  • SH2-B isoforms homodimerize via a unique amino-terminal domain.

Related Experiment Videos

  • SH2-B and APS SH2 domains bind JAK2 at Tyr813.
  • Dimerization of SH2-B/APS with JAK2 can lead to heterotetrameric complexes.
  • Low expression levels promote JAK2 transactivation, while high levels inhibit kinase activity.

    • Conclusions:

    • SH2-B and APS homodimerization and heterodimerization provide mechanisms for regulating JAK2 activity.
    • These dimerization events offer intracellular control over cytokine and growth factor receptor signaling.
    • The concentration-dependent effects allow for potentiation or attenuation of signaling pathways.