Source:http://linkedlifedata.com/resource/pubmed/id/19935774
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
|
pubmed:dateCreated |
2009-12-3
|
pubmed:abstractText |
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.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Dyneins,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNX1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SNX6 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Sorting Nexins,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/dynactin
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
1748-7838
|
pubmed:author | |
pubmed:issnType |
Electronic
|
pubmed:volume |
19
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1334-49
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:19935774-Dyneins,
pubmed-meshheading:19935774-Endosomes,
pubmed-meshheading:19935774-HeLa Cells,
pubmed-meshheading:19935774-Humans,
pubmed-meshheading:19935774-Intracellular Membranes,
pubmed-meshheading:19935774-Microtubule-Associated Proteins,
pubmed-meshheading:19935774-Microtubules,
pubmed-meshheading:19935774-Protein Transport,
pubmed-meshheading:19935774-Sorting Nexins,
pubmed-meshheading:19935774-Vesicular Transport Proteins,
pubmed-meshheading:19935774-trans-Golgi Network
|
pubmed:year |
2009
|
pubmed:articleTitle |
The retromer component SNX6 interacts with dynactin p150(Glued) and mediates endosome-to-TGN transport.
|
pubmed:affiliation |
Key Laboratory of Molecular and Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|