Retromer recycles vacuolar sorting receptors from the trans-Golgi network

• Verfasst von: Sturm, Silke [VerfasserIn]
• Verfasst von: Langhans, Markus [VerfasserIn]
• Verfasst von: Viotti, Corrado [VerfasserIn]
• Verfasst von: Scheuring, David [VerfasserIn]
• Verfasst von: Hillmer, Stefan [VerfasserIn]
• Verfasst von: Robinson, David G. [VerfasserIn]
• Verfasst von: Pimpl, Peter [VerfasserIn]
• Titel: Retromer recycles vacuolar sorting receptors from the trans-Golgi network
• Verf.angabe: Silke Niemes, Markus Langhans, Corrado Viotti, David Scheuring, Melody San Wan Yan, Liwen Jiang, Stefan Hillmer, David G. Robinson and Peter Pimpl
• Jahr: 2010
• Jahr des Originals: 2009
• Umfang: 15 S.
• Fussnoten: Online published: 4 November 2009 ; Gesehen am 22.05.2017
• Titel Quelle: Enthalten in: The plant journal
• Ort Quelle: Oxford [u.a.] : Wiley-Blackwell, 1991
• Jahr Quelle: 2010
• Band/Heft Quelle: 61(2010), 1, Seite 107-121
• ISSN Quelle: 1365-313X
• DOI: doi:10.1111/j.1365-313X.2009.04034.x
• Datenträger: Online-Ressource
• Sprache: eng
• Sach-SW: early endosomes
• Sach-SW: pre-vacuolar compartment
• Sach-SW: retromer
• Sach-SW: sorting nexins
• Sach-SW: trans-Golgi network
• Sach-SW: vacuolar sorting receptor
• K10plus-PPN: 155888324X

Abstract

Receptor-mediated sorting processes in the secretory pathway of eukaryotic cells rely on mechanisms to recycle the receptors after completion of transport. Based on this principle, plant vacuolar sorting receptors (VSRs) are thought to recycle after dissociating of receptor-ligand complexes in a pre-vacuolar compartment. This recycling is mediated by retromer, a cytosolic coat complex that comprises sorting nexins and a large heterotrimeric subunit. To analyse retromer-mediated VSR recycling, we have used a combination of immunoelectron and fluorescence microscopy to localize the retromer components sorting nexin 1 (SNX1) and sorting nexin 2a (SNX2a) and the vacuolar sorting protein VPS29p. All retromer components localize to the trans-Golgi network (TGN), which is considered to represent the early endosome of plants. In addition, we show that inhibition of retromer function in vivo by expression of SNX1 or SNX2a mutants as well as transient RNAi knockdown of all sorting nexins led to accumulation of the VSR BP80 at the TGN. Quantitative protein transport studies and live-cell imaging using fluorescent vacuolar cargo molecules revealed that arrival of these VSR ligands at the vacuole is not affected under these conditions. Based on these findings, we propose that the TGN is the location of retromer-mediated recycling of VSRs, and that transport towards the lytic vacuole downstream of the TGN is receptor-independent and occurs via maturation, similar to transition of the early endosome into the late endosome in mammalian cells.