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CLIP-170 is essential for MTOC repositioning during T cell activation by regulating dynein localisation on the cell

Wei Ming Lim1, Yuma Ito1, Kumiko Sakata-Sogawa2

  • 1School of Life Science and Technology, Tokyo Institute of Technology, Nagatsuta-cho, Midori, Yokohama, Kanagawa, 226-8501, Japan.

Scientific Reports
|November 30, 2018
PubMed

Insights

Cytoplasmic linker protein 170 (CLIP-170) is crucial for microtubule-organizing centre (MTOC) repositioning during T cell activation. Its phosphorylation regulates dynein motor protein localization, essential for T cell function and interleukin-2 expression.

Area of Science:

  • Immunology
  • Cell Biology
  • Molecular Biology

Background:

  • T cell activation involves repositioning of the microtubule-organizing centre (MTOC) to the immunological synapse.
  • The precise molecular mechanisms governing MTOC repositioning remain incompletely understood.

Purpose of the Study:

  • To investigate the role of cytoplasmic linker protein 170 (CLIP-170) in MTOC repositioning during T cell activation.
  • To elucidate the molecular mechanism by which CLIP-170 influences MTOC dynamics and T cell function.

Main Methods:

  • Utilized fluorescence imaging to observe MTOC repositioning and protein localization in T cells.
  • Investigated the impact of CLIP-170 phosphorylation inhibition on MTOC movement and interleukin-2 (IL-2) expression.
  • Analyzed the colocalization and movement patterns of dynein motor proteins in relation to CLIP-170.

Main Results:

  • CLIP-170 was identified as a key regulator of MTOC repositioning.
  • Inhibition of CLIP-170 phosphorylation impaired MTOC repositioning and reduced IL-2 expression.
  • T cell stimulation promoted dynein colocalization with CLIP-170 and enhanced its minus-end-directed movement towards the cell center.
  • Dynein movement dynamics suggest it actively pulls microtubules and the MTOC.

Conclusions:

  • CLIP-170 plays an essential role in MTOC repositioning by regulating dynein localization and function at the immunological synapse.
  • Phosphorylated CLIP-170 is critical for dynein recruitment and relocation, facilitating T cell activation.
  • The coordinated action of CLIP-170 and dynein is vital for the full activation of T cells.

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