Volume 19, No 12, Dec 2009
ISSN: 1001-0602
EISSN: 1748-7838 2018
impact factor 17.848*
(Clarivate Analytics, 2019)
Volume 19 Issue 12, December 2009: 1334-1349
ORIGINAL ARTICLES
The retromer component SNX6 interacts with dynactin p150Glued and mediates endosome-to-TGN transport
Zhi Hong1,2,*, Yanrui Yang1,*, Cheng Zhang1, Yang Niu1,2, Ke Li1,2, Xi Zhao1,2 and Jia-Jia Liu1
1Key Laboratory of Molecular and Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China
2Graduate School, Chinese Academy of Sciences, Beijing 100039, China
Correspondence: Jia-Jia Liu,(jjliu@genetics.ac.cn)
The retromer is a protein complex that mediates retrograde transport of transmembrane cargoes from endosomes to the
trans-Golgi network (TGN). It is comprised of a cargo-selection subcomplex of Vps26, Vps29 and Vps35 and a membrane-binding coat subcomplex of sorting nexins (SNXs). Previous studies identified SNX1/2 as one of the components of the SNX subcomplex, and SNX5/6 as candidates for the second SNX. How the retromer-associated cargoes are recognized and transported by molecular motors are largely unknown. In this study, we found that one of SNX1/2's dimerization partners, SNX6, interacts with the p150
Glued subunit of the dynein/dynactin motor complex. We present evidence that SNX6 is a component of the retromer, and that recruitment of the motor complex to the membrane-associated retromer requires the SNX6-p150
Glued interaction. Disruption of the SNX6-p150
Glued interaction causes failure in formation and detachment of the tubulovesicular sorting structures from endosomes and results in block of CI-MPR retrieval from endosomes to the TGN. These observations indicate that in addition to SNX1/2, SNX6 in association with the dynein/dynactin complex drives the formation and movement of tubular retrograde intermediates.
Cell Research (2009) 19:1334-1349. doi: 10.1038/cr.2009.130; published online 24 November 2009
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