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Endosomal trafficking of the Menkes copper ATPase ATP7A is mediated by vesicles containing the Rab7 and Rab5 GTPase proteins

Pascale, M. C., Franceschelli, S., Moltedo, O., Belleudi, F., Torrisi, M. R., Bucci, C., La Fontaine, Sharon, Mercer, Julian and Leone, A. 2003, Endosomal trafficking of the Menkes copper ATPase ATP7A is mediated by vesicles containing the Rab7 and Rab5 GTPase proteins, Experimental cell research, vol. 291, no. 2, pp. 377-385, doi: 10.1016/j.yexcr.2003.07.001.

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Title Endosomal trafficking of the Menkes copper ATPase ATP7A is mediated by vesicles containing the Rab7 and Rab5 GTPase proteins
Author(s) Pascale, M. C.
Franceschelli, S.
Moltedo, O.
Belleudi, F.
Torrisi, M. R.
Bucci, C.
La Fontaine, SharonORCID iD for La Fontaine, Sharon orcid.org/0000-0002-9948-074X
Mercer, Julian
Leone, A.
Journal name Experimental cell research
Volume number 291
Issue number 2
Start page 377
End page 385
Publisher Academic Press
Place of publication San Diego, Calif
Publication date 2003-12-10
ISSN 0014-4827
1090-2422
Keyword(s) MNK protein
rab proteins
vesicular trafficking
copper transport
Chinese hamster ovary cells
trans-Golgi network
Summary The Cu-ATPase ATP7A (MNK) is localized in the trans-Golgi network (TGN) and relocalizes in the plasma membrane via vesicle-mediated traffic following exposure of the cells to high concentrations of copper. Rab proteins are organelle-specific GTPases, markers of different endosomal compartments; their role has been recently reviewed (Trends Cell Biol. 11(2001) 487). In this article we analyze the endosomal pathway of trafficking of the MNK protein in stably transfected clones of CHO cells, expressing chimeric Rab5-myc or Rab7-myc proteins, markers of early or late endosome compartments, respectively. We demonstrate by immunofluorescence and confocal and electron microscopy techniques that the increase in the concentration of copper in the medium (189 μM) rapidly induces a redistribution of the MNK protein from early sorting endosomes, positive for Rab5-myc protein, to late endosomes, containing the Rab7-myc protein. Cell fractionation experiments confirm these results; i.e., the MNK protein is recruited to the endosomal fraction on copper stimulation and colocalizes with Rab5 and Rab7 proteins. These findings allow the first characterization of the vesicles involved in the intracellular routing of the MNK protein from the TGN to the plasma membrane, a key mechanism allowing appropriate efflux of copper in cells grown in high concentrations of the metal.


Language eng
DOI 10.1016/j.yexcr.2003.07.001
Field of Research 060108 Protein Trafficking
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2003, Elsevier Inc.
Persistent URL http://hdl.handle.net/10536/DRO/DU:30008601

Document type: Journal Article
Collection: School of Biological and Chemical Sciences
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