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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2006-5-10
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pubmed:abstractText |
The biogenesis of endothelial-specific Weibel-Palade bodies (WPB) is poorly understood, despite their key role in both haemostasis and inflammation. Biogenesis of specialized organelles of haemopoietic cells is often adaptor protein complex 3-dependent (AP-3-dependent), and AP-3 has previously been shown to play a role in the trafficking of both WPB membrane proteins, P-selectin and CD63. However, WPB are thought to form at the trans Golgi network (TGN), which is inconsistent with a role for AP-3, which operates in post-Golgi trafficking. We have therefore investigated in detail the mechanisms of delivery of these two membrane proteins to WPB. We find that P-selectin is recruited to forming WPB in the trans-Golgi by AP-3-independent mechanisms that use sorting information within both the cytoplasmic tail and the lumenal domain of the receptor. In contrast, CD63 is recruited to already-budded WPB by an AP-3-dependent route. These different mechanisms of recruitment lead to the presence of distinct immature and mature populations of WPB in human umbilical vein endothelial cells (HUVEC).
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Protein Complex 3,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD63,
http://linkedlifedata.com/resource/pubmed/chemical/CD63 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cd63 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/P-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1398-9219
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
647-62
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:16683915-Adaptor Protein Complex 3,
pubmed-meshheading:16683915-Amino Acid Sequence,
pubmed-meshheading:16683915-Animals,
pubmed-meshheading:16683915-Antigens, CD,
pubmed-meshheading:16683915-Antigens, CD63,
pubmed-meshheading:16683915-Base Sequence,
pubmed-meshheading:16683915-Cells, Cultured,
pubmed-meshheading:16683915-DNA-Binding Proteins,
pubmed-meshheading:16683915-Endothelium, Vascular,
pubmed-meshheading:16683915-Humans,
pubmed-meshheading:16683915-Leukocyte Rolling,
pubmed-meshheading:16683915-Mice,
pubmed-meshheading:16683915-Mice, Inbred C57BL,
pubmed-meshheading:16683915-Mice, Mutant Strains,
pubmed-meshheading:16683915-Microscopy, Electron,
pubmed-meshheading:16683915-Models, Biological,
pubmed-meshheading:16683915-P-Selectin,
pubmed-meshheading:16683915-Platelet Membrane Glycoproteins,
pubmed-meshheading:16683915-Protein Sorting Signals,
pubmed-meshheading:16683915-Protein Structure, Tertiary,
pubmed-meshheading:16683915-Protein Transport,
pubmed-meshheading:16683915-RNA, Small Interfering,
pubmed-meshheading:16683915-Recombinant Fusion Proteins,
pubmed-meshheading:16683915-Transcription Factors,
pubmed-meshheading:16683915-Weibel-Palade Bodies,
pubmed-meshheading:16683915-trans-Golgi Network
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pubmed:year |
2006
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pubmed:articleTitle |
P-selectin and CD63 use different mechanisms for delivery to Weibel-Palade bodies.
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pubmed:affiliation |
MRC Laboratory of Molecular Cell Biology, Cell Biology Unit, University College London, Gower Street, London WC1E 6BT, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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