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A more recent version of this article appeared on February 1, 2003
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Submitted on April 18, 2002
Revised on October 4, 2002
Accepted on October 21, 2002
1 Departament de Biologia Cellular i Anatomia Patològica, Facultat de Medicina, Institut d'Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Universitat de Barcelona, E-08036 Barcelona, Spain
2 Departament de Biologia Cellular i Anatomia Patològica, Facultat de Medicina, Institut d'Investigacions Biomèdiques August Pi i Sunyer (IDIBAPS), Universitat de Barcelona, E-08036 Barcelona, Spain(present address: Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, London WC2A 3PX)
3 Serveis CientificoTècnics, Universitat de Barcelona, E-08028 Barcelona, Spain
4 School of Biosciences, Molecular Cell Division, University of Birmingham, Birmingham B15-2TT, United Kingdom
5 Centro de Investigación, Hospital La Fe, E-46009 Valencia, Spain
6 Dept. of Biological Science, Graduate School of Science, Hiroshima University, 739-8526 Hiroshima, Japan
7 Dept. of Biology, University of California San Diego, La Jolla, California 92093, USA
* Corresponding author. E-mail address: egea{at}medicina.ub.es.
We have previously reported that actin filaments are involved in protein transport from the Golgi complex to the endoplasmic reticulum. Here we examined whether myosin motors or actin comets mediate this transport. To address this issue we have used, on one hand, a combination of specific inhibitors such as BDM (2,3-butanedione monoxime) and ML7 (1-[5-isoquinoline sulfonyl]-2-methyl piperazine), which inhibit myosin and the phosphorylation of myosin II by the myosin light chain kinase, respectively; and a mutant of the nonmuscle myosin II regulatory light chain, which cannot be phosphorylated (MRLC2AA). On the other hand, actin comet tails were induced by the overexpression of phosphatidylinositol phosphate 5-kinase (PIP5K). Cells treated with BDM/ML7 or those that express the MRLC2AA mutant revealed a significant reduction in the BFA-induced fusion of Golgi enzymes with the ER. This delay was not caused by an alteration in the formation of the BFA-induced tubules from the Golgi complex. In addition, the Shiga toxin fragment B transport from the Golgi complex to the ER was also altered. This impairment in the retrograde protein transport was not due to depletion of intracellular calcium stores or the activation of Rho kinase. Neither the reassembly of the Golgi complex after BFA removal nor VSV-G transport from ER to the Golgi was altered in cells treated with BDM/ML7 or expressing MRLC2AA. Finally, transport carriers containing Shiga toxin did not move into the cytosol at the tips of comet tails of polymerizing actin. Collectively, the results indicate that: (1) myosin motors move to transport carriers from the Golgi complex to the ER along actin filaments; (2) nonmuscle myosin II mediates in this process; and (3) actin comets are not involved in retrograde transport.
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