Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/24654
Title: Myosin motors and not actin comets are mediators of the actin-based Golgi-to-endoplasmic reticulum protein transport
Author: Durán Serrano, Juan Manuel
Valderrama i Alfonso, Ferran
Castel i Gil, Susanna
Magdalena, Juana
Tomás, Mónica
Hosoya, Hiroshi
Renau Piqueras, Jaime
Malhotra, Vivek
Egea Guri, Gustavo
Keywords: Aparell de Golgi
Reticle endoplasmàtic
Proteïnes
Transport biològic
Citologia
Golgi apparatus
Endoplasmic reticulum
Proteins
Biological transport
Cytology
Issue Date: 2003
Publisher: American Society for Cell Biology
Abstract: We have previously reported that actin filaments are involved in protein transport from the Golgi complex to the endoplasmic reticulum. Herein, 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 2,3-butanedione monoxime (BDM) and 1-[5-isoquinoline sulfonyl]-2-methyl piperazine (ML7), 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. Cells treated with BDM/ML7 or those that express the MRLC2AA mutant revealed a significant reduction in the brefeldin A (BFA)-induced fusion of Golgi enzymes with the endoplasmic reticulum (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 to 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.
Note: Reproducció del document publicat a: http://dx.doi.org/10.1091/mbc.E02-04-0214
It is part of: Molecular Biology of the Cell, 2003, vol. 14, núm. 2, p. 445-459
Related resource: http://dx.doi.org/10.1091/mbc.E02-04-0214
URI: http://hdl.handle.net/2445/24654
ISSN: 1059-1524
Appears in Collections:Articles publicats en revistes (Biomedicina)

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