Change search
ReferencesLink to record
Permanent link

Direct link
SNX18 is an SNX9 paralog that acts as a membrane tubulator in AP-1-positive endosomal trafficking.
Umeå University, Faculty of Medicine, Medical Biochemistry and Biophsyics.
Umeå University, Faculty of Medicine, Medical Biochemistry and Biophsyics.
Umeå University, Faculty of Medicine, Medical Biochemistry and Biophsyics.
2008 (English)In: Journal of Cell Science, ISSN 0021-9533, Vol. 121, no Pt 9, 1495-505 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2008. Vol. 121, no Pt 9, 1495-505 p.
URN: urn:nbn:se:umu:diva-9591PubMedID: 18411244OAI: diva2:149262
Available from: 2008-04-29 Created: 2008-04-29 Last updated: 2012-02-08Bibliographically approved
In thesis
1. Membrane-remodeling by SNX18 in endosomal transport and autophagy
Open this publication in new window or tab >>Membrane-remodeling by SNX18 in endosomal transport and autophagy
2012 (English)Doctoral thesis, comprehensive summary (Other academic)
Alternative title[sv]
SNX18 - ett membranaktivt protein vid endosomal transport och autofagi
Abstract [en]

The intracellular space of eukaryotic cells is subdivided into functionally distinct membrane-enclosed organelles. Regulation of these intracellular membranes requires an intricate network of specialized lipids and proteins that maintain organellar integrity and mediate transport between organelles. Proteins of the sorting nexin (SNX) family are membrane-binding regulators of transport events within the endomembrane system. The endomembrane system includes organelles associated with endocytic, secretory and degradative processes in the cell. The aims of this thesis were to functionally characterize SNX18 and SNX33, members of the SNX9-subfamily of sorting nexins, and to elucidate the role of SNX18 in autophagy.

We demonstrated that all three proteins in the SNX9-family are capable of both membrane binding and remodeling, and interact with the membrane scission enzyme dynamin. We found that SNX18 localizes to endosomal structures in the endomembrane system, together with several identified factors previously described as regulators of endosomal transport. These results indicate that SNX18 mediates budding of membrane carriers in endosomal trafficking. In addition to this, knockdown of SNX18 in cultured cells was found to inhibit autophagy. Autophagy is a catabolic process by which cells degrade and recycle cellular components. It is a cellular response to various stress conditions such as oxidative stress, nutrient deprivation and infections. The components destined for degradation by autophagy are sequestered into a double-membrane structure called the autophagosome in which they are delivered to the lysosome. SNX18 interacts directly with proteins connected to autophagosome formation. Moreover, we demonstrated that the membrane-remodeling capability of SNX18 is a prerequisite for autophagosome formation.

Taken together, our results lead to the conclusions that SNX18 remodels cellular membranes during formation of carriers for endosomal transport and that it is a positive regulator of autophagy and autophagosome formation.

Place, publisher, year, edition, pages
Department of Medical Biochemistry and Biophysics, Umeå University, 2012. 42 p.
Umeå University medical dissertations, ISSN 0346-6612 ; 1478
Sorting nexin, SNX9-family, SNX18, endosomal transport, autophagy
National Category
Cell and Molecular Biology
Research subject
Medical Biochemistry
urn:nbn:se:umu:diva-51999 (URN)978-91-7459-366-2 (ISBN)
Public defence
2012-02-29, KB3A9, KBC-huset, Linnaeus väg, Umeå Universitet, Umeå, 09:00 (English)
Available from: 2012-02-08 Created: 2012-02-07 Last updated: 2012-02-08Bibliographically approved

Open Access in DiVA

No full text

Other links


Search in DiVA

By author/editor
Håberg, KarinLundmark, RichardCarlsson, Sven
By organisation
Medical Biochemistry and Biophsyics

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 170 hits
ReferencesLink to record
Permanent link

Direct link