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Structure of the N-terminal domain of the FOP (FGFR1OP) protein and implications for its dimerization and centrosomal

Aleksandra Mikolajka1, Xiumin Yan, Grzegorz M Popowicz

  • 1Max Planck Institute of Biochemistry, D-82152 Martinsried, Germany.

Journal of Molecular Biology
|May 13, 2006
PubMed

Insights

The FOP protein, a partner of FGFR1, anchors microtubules at the centrosome. Its N-terminal domain structure reveals a dimerization interface crucial for its cellular role.

Area of Science:

  • Cell Biology
  • Structural Biology
  • Molecular Oncology

Background:

  • Fibroblast growth factor receptor 1 (FGFR1) oncogene partner (FOP) is a centrosomal protein.
  • FOP was identified as an FGFR1 fusion partner in stem cell myeloproliferative disorders.
  • FOP contains a Lis-homology (LisH) motif implicated in microtubule dynamics and cell division.

Purpose of the Study:

  • To elucidate the structural basis of FOP dimerization.
  • To investigate the role of the N-terminal domain in FOP's centrosomal localization.
  • To understand the structural contribution of the LisH motif to FOP function.

Main Methods:

  • X-ray crystallography at 1.6A resolution.
  • Protein structure determination and analysis.
  • Biochemical assays to assess dimerization and localization.

Main Results:

  • The crystal structure of the FOP N-terminal dimerization domain was determined.
  • The structure reveals an alpha-helical bundle forming a two-chain antiparallel dimer.
  • The LisH domain is centrally located within the dimer interface.
  • A longer N-terminal segment is necessary for FOP dimerization and centrosomal localization.

Conclusions:

  • The N-terminal domain of FOP forms a stable dimer through an alpha-helical bundle.
  • The LisH motif is integral to the FOP dimerization interface.
  • The FOP N-terminal region plays a critical role in mediating centrosomal localization.

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