Microtubule plus ends, motors, and traffic of Golgi membranes

Biochim Biophys Acta. 2005 Jul 10;1744(3):316-24. doi: 10.1016/j.bbamcr.2005.05.001.


The intimate link between microtubule (MT) organization and the components of the secretory pathway has suggested that MT-based motility is an essential component of vesicular membrane transport and membrane polarization. The molecular details of these processes are still under investigation; however, a novel class of MT plus end-binding proteins shed new light on transport between the endoplasmic reticulum (ER) and Golgi apparatus. The dynactin complex, an initial member of this family, shares localization and live-cell imaging phenotypes with other plus end-binding proteins such as CLIP-170 and EB1. In addition, dynactin has been shown to mediate the binding of ER-Golgi transport vesicles to MTs through a regulated MT-binding motif in p150(Glued). Whereas the plus end-binding activity of CLIP-170 and EB1 has been linked to the regulation of dynamic instability, the plus end binding of dynactin is implicated in a search-capture mechanism for dynein-dependent cargoes. An examination of dynactin's role in ER-Golgi transport suggests that plus end binding could be a reflection of fundamental membrane transport mechanisms.

Publication types

  • Review

MeSH terms

  • Animals
  • Cytoplasm / metabolism
  • Dynactin Complex
  • Endoplasmic Reticulum / metabolism*
  • Intracellular Membranes / metabolism
  • Microtubule-Associated Proteins / analysis
  • Microtubule-Associated Proteins / metabolism*
  • Microtubules / chemistry
  • Microtubules / metabolism*
  • Protein Transport
  • trans-Golgi Network / metabolism*


  • Dynactin Complex
  • Microtubule-Associated Proteins