TIP150 interacts with and targets MCAK at the microtubule plus ends

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Updated: Jun 22, 2026

Self-Assembly of Microtubule Tactoids
08:49

Self-Assembly of Microtubule Tactoids

Published on: June 23, 2022

Kai Jiang1, Jianyu Wang, Jing Liu

  • 1Anhui Key Laboratory for Cellular Dynamics and Chemical Biology, University of Science and Technology of China, Hefei 230027, China.

EMBO Reports
|June 23, 2009
PubMed

Insights

TIP150 is a novel plus-end tracking protein (+TIP) that binds to EB1 and MCAK, crucial for microtubule dynamics during cell division. It facilitates EB1-dependent MCAK loading, regulating microtubule plus-end dynamics.

Area of Science:

  • Cell Biology
  • Cytoskeleton Dynamics
  • Molecular Mechanisms

Background:

  • Microtubule (MT) cytoskeleton is vital for cellular processes like morphogenesis and cell division.
  • Plus-end tracking proteins (+TIPs) regulate MT dynamics at growing plus ends, essential for cell division and migration.
  • The precise mechanisms of +TIP regulation at spindle and astral MTs remain unclear.

Purpose of the Study:

  • To identify and characterize a novel +TIP involved in MT plus-end regulation.
  • To elucidate the molecular interactions of TIP150 with known MT-associated proteins.
  • To understand TIP150's role in controlling MT dynamics at spindle and astral MTs.

Main Methods:

  • In vitro binding assays to study protein interactions.
  • In vivo co-localization studies using microscopy.
  • Gene suppression techniques (e.g., siRNA) to assess protein function.
  • Investigating the effect of phosphorylation on protein interactions.

Main Results:

  • TIP150 identified as a new +TIP, binding to EB1 and co-localizing with it at MT plus ends.
  • EB1 suppression abolishes TIP150 localization to MT plus ends.
  • TIP150 binds to MCAK, an MT depolymerase, and its suppression reduces MCAK plus-end localization.
  • Aurora B-mediated phosphorylation disrupts the TIP150-MCAK interaction in vitro.

Conclusions:

  • TIP150 acts as a scaffold, facilitating EB1-dependent recruitment of MCAK to MT plus ends.
  • TIP150 plays a critical role in orchestrating MT plus-end dynamics.
  • This provides new insights into the molecular regulation of MT dynamics during cell division.

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