Journal
EXPERIMENTAL CELL RESEARCH
Volume 316, Issue 20, Pages 3454-3467Publisher
ELSEVIER INC
DOI: 10.1016/j.yexcr.2010.07.020
Keywords
Dynamin; Fission; Golgi complex; Peroxisomes
Categories
Funding
- German Research Foundation (DFG) [SCHR 518/6-1, 2, Sonderforschungsbereich 593]
- Portuguese Foundation for Science and Technology (FCT) [REEQ/1023/BIO/2005, PTDC/BIA-BCM/71932/2006, SFRH/BD/37647/2007]
- University of Aveiro
- University of Marburg
- Fundação para a Ciência e a Tecnologia [SFRH/BD/37647/2007, PTDC/BIA-BCM/71932/2006] Funding Source: FCT
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The final step in the liberation of secretory vesicles from the trans-Golgi network (TGN) involves the mechanical action of the large GTPase dynamin as well as conserved dynamin-independent fission mechanisms, e.g. mediated by Brefeldin A-dependent ADP-ribosylated substrate (BARS). Another member of the dynamin family is the mammalian dynamin-like protein 1 (DLP1/Drp1) that is known to constrict and tubulate membranes, and to divide mitochondria and peroxisomes. Here, we examined a potential role for DLP1 at the Golgi complex. DLP1 localized to the Golgi complex in some but not all cell lines tested, thus explaining controversial reports on its cellular distribution. After silencing of DLP1, an accumulation of the apical reporter protein YFP-GL-GPI, but not the basolateral reporter VSVG-SP-GFP at the Golgi complex was observed. A reduction in the transport of YFP-GL-GPI to the plasma membrane was confirmed by surface immunoprecipitation and TGN-exit assays. In contrast, YFP-GL-GPI trafficking was not disturbed in cells silenced for BARS, which is involved in basolateral sorting and trafficking of VSVG-SP-GFP in COS-7 cells. Our data indicate a new role for DLP1 at the Golgi complex and thus a role for DLP1 as a novel component of the apical sorting machinery at the TGN is discussed. (C) 2010 Elsevier Inc. All rights reserved.
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