|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
11
|
|
pubmed:dateCreated |
2006-10-17
|
|
pubmed:abstractText |
Exit of soluble secretory proteins from the endoplasmic reticulum (ER) can occur by receptor-mediated export as exemplified by blood coagulation factors V and VIII. Their efficient secretion requires the membrane lectin ER Golgi intermediate compartment protein-53 (ERGIC-53) and its soluble luminal interaction partner multiple coagulation factor deficiency protein 2 (MCFD2), which form a cargo receptor complex in the early secretory pathway. ERGIC-53 also interacts with the two lysosomal glycoproteins cathepsin Z and cathepsin C. Here, we tested the subunit interdependence and cargo selectivity of ERGIC-53 and MCFD2 by short interference RNA-based knockdown. In the absence of ERGIC-53, MCFD2 was secreted, whereas knocking down MCFD2 had no effect on the localization of ERGIC-53. Cargo binding properties of the ERGIC-53/MCFD2 complex were analyzed in vivo using yellow fluorescent protein fragment complementation. We found that MCFD2 is dispensable for the binding of cathepsin Z and cathepsin C to ERGIC-53. The results indicate that ERGIC-53 can bind cargo glycoproteins in an MCFD2-independent fashion and suggest that MCFD2 is a recruitment factor for blood coagulation factors V and VIII.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Brefeldin A,
http://linkedlifedata.com/resource/pubmed/chemical/CTSK protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CTSZ protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin C,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin K,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin Z,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/LMAN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MCFD2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Mannose-Binding Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/yellow fluorescent protein, Bacteria
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
1398-9219
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
7
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1473-81
|
|
pubmed:dateRevised |
2009-11-19
|
|
pubmed:meshHeading |
pubmed-meshheading:17010120-Bacterial Proteins,
pubmed-meshheading:17010120-Brefeldin A,
pubmed-meshheading:17010120-Cathepsin C,
pubmed-meshheading:17010120-Cathepsin K,
pubmed-meshheading:17010120-Cathepsin Z,
pubmed-meshheading:17010120-Cathepsins,
pubmed-meshheading:17010120-Endoplasmic Reticulum,
pubmed-meshheading:17010120-HeLa Cells,
pubmed-meshheading:17010120-Humans,
pubmed-meshheading:17010120-Luminescent Proteins,
pubmed-meshheading:17010120-Mannose-Binding Lectins,
pubmed-meshheading:17010120-Membrane Proteins,
pubmed-meshheading:17010120-Protein Binding,
pubmed-meshheading:17010120-Protein Interaction Mapping,
pubmed-meshheading:17010120-Protein Transport,
pubmed-meshheading:17010120-RNA, Small Interfering,
pubmed-meshheading:17010120-Vesicular Transport Proteins
|
|
pubmed:year |
2006
|
|
pubmed:articleTitle |
Cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex.
|
|
pubmed:affiliation |
Biozentrum, University of Basel, CH-4056 Basel, Switzerland.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
|
