Molecular Pathway of Microtubule Organization at the Golgi Apparatus

Dev Cell. 2016 Oct 10;39(1):44-60. doi: 10.1016/j.devcel.2016.08.009. Epub 2016 Sep 22.


The Golgi apparatus controls the formation of non-centrosomal microtubule arrays important for Golgi organization, polarized transport, cell motility, and cell differentiation. Here, we show that CAMSAP2 stabilizes and attaches microtubule minus ends to the Golgi through a complex of AKAP450 and myomegalin. CLASPs stabilize CAMSAP2-decorated microtubules but are not required for their Golgi tethering. AKAP450 is also essential for Golgi microtubule nucleation, and myomegalin and CDK5RAP2 but not CAMSAP2 contribute to this function. In the absence of centrosomes, AKAP450- and CAMSAP2-dependent pathways of microtubule minus-end organization become dominant, and the presence of at least one of them is needed to maintain microtubule density. Strikingly, a compact Golgi can be assembled in the absence of both centrosomal and Golgi microtubules. However, CAMSAP2- and AKAP450-dependent Golgi microtubules facilitate Golgi reorientation and cell invasion in a 3D matrix. We propose that Golgi-anchored microtubules are important for polarized cell movement but not for coalescence of Golgi membranes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • A Kinase Anchor Proteins / metabolism
  • Cell Line
  • Cell Movement / drug effects
  • Cell Polarity / drug effects
  • Centrioles / metabolism
  • Cytoskeletal Proteins / metabolism
  • Golgi Apparatus / drug effects
  • Golgi Apparatus / metabolism*
  • Humans
  • Imaging, Three-Dimensional
  • Intracellular Membranes / metabolism
  • Microtubule-Associated Proteins / metabolism
  • Microtubules / drug effects
  • Microtubules / metabolism*
  • Protein Binding / drug effects
  • Protein Stability / drug effects
  • Pyrimidines / pharmacology
  • Signal Transduction* / drug effects
  • Sulfones / pharmacology
  • Tubulin / metabolism


  • A Kinase Anchor Proteins
  • AKAP9 protein, human
  • Camsap3 protein, human
  • Cytoskeletal Proteins
  • Microtubule-Associated Proteins
  • Pyrimidines
  • Sulfones
  • Tubulin
  • centrinone