Microtubule plus ends, motors, and traffic of Golgi membranes.
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.
Vaughan
Kevin T
KT
Department of Biological Sciences, P.O. Box 369, University of Notre Dame, Notre Dame, IN 46556, USA. Vaughan.4@nd.edu
D000818:Animals; D003593:Cytoplasm / Q000378:metabolism; D000072159:Dynactin Complex; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D007425:Intracellular Membranes / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000032:analysis / Q000378:metabolism*; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism*; D021381:Protein Transport; D021601:trans-Golgi Network / Q000378:metabolism*
D000072159:Dynactin Complex; D008869:Microtubule-Associated Proteins