Myosin II is involved in the production of constitutive transport vesicles from the TGN. Academic Article uri icon

Overview

abstract

  • The participation of nonmuscle myosins in the transport of organelles and vesicular carriers along actin filaments has been documented. In contrast, there is no evidence for the involvement of myosins in the production of vesicles involved in membrane traffic. Here we show that the putative TGN coat protein p200 (Narula, N., I. McMorrow, G. Plopper, J. Doherty, K.S. Matlin, B. Burke, and J.L. Stow. 1992. J. Cell Biol. 114: 1113-1124) is myosin II. The recruitment of myosin II to Golgi membranes is dependent on actin and is regulated by G proteins. Using an assay that studies the release of transport vesicles from the TGN in vitro, we provide functional evidence that p200/myosin is involved in the assembly of basolateral transport vesicles carrying vesicular stomatitis virus G protein (VSVG) from the TGN of polarized MDCK cells. The 50% reduced efficiency in VSVG vesicle release from the TGN in vitro after depletion of p200/myosin II could be reestablished to control levels by the addition of purified nonmuscle myosin II. Several inhibitors of the actin-stimulated ATPase activity of myosin specifically inhibited the release of VSVG-containing vesicles from the TGN.

publication date

  • July 28, 1997

Research

keywords

  • Golgi Apparatus
  • Intracellular Membranes
  • Membrane Glycoproteins
  • Myosins

Identity

PubMed Central ID

  • PMC2138203

Scopus Document Identifier

  • 0040971539

Digital Object Identifier (DOI)

  • 10.1083/jcb.138.2.291

PubMed ID

  • 9230072

Additional Document Info

volume

  • 138

issue

  • 2