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The nucleolar PICT-1/GLTSCR2 protein forms homo-oligomers

Tatyana Borodianskiy-Shteinberg1, Inna Kalt1, Sarit Kipper1

  • 1The Mina and Everard Goodman Faculty of Life Sciences, Bar Ilan University, Ramat-Gan, Israel 5290002.

Journal of Molecular Biology
|April 17, 2014
PubMed

Insights

Protein interacting with carboxyl terminus 1 (PICT-1) self-associates, forming dimers. This finding adds complexity to understanding PICT-1

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The function of human protein interacting with carboxyl terminus 1 (PICT-1), also known as GLTSCR2, remains unclear.
  • PICT-1 has contradictory roles in cancer, acting as either a tumor suppressor or oncogene.

Purpose of the Study:

  • To investigate the self-interaction of PICT-1.
  • To identify the domains responsible for PICT-1 self-association.

Main Methods:

  • Yeast two-hybrid assays
  • Co-immunoprecipitation
  • Fluorescence resonance energy transfer (FRET)
  • In vitro microfluidic affinity binding assays
  • Glutaraldehyde cross-linking
  • Gel-filtration assays

Main Results:

  • PICT-1 self-associates in yeast and mammalian cells.
  • The carboxy-terminal domain mediates PICT-1 self-interaction.
  • PICT-1 forms dimers and potentially higher-order complexes.

Conclusions:

  • Demonstrated PICT-1 self-association provides new insights into its complex functions.
  • Understanding PICT-1's self-interaction is crucial for elucidating its role in cellular processes and cancer.
Keywords:
glioma tumor suppressor candidate region 2 gene product, GLTSCR2nucleolusoligomerp53protein interacting with carboxyl terminus 1, PICT-1

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