| pubmed-article:15086781 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15086781 | lifeskim:mentions | umls-concept:C0887838 | lld:lifeskim |
| pubmed-article:15086781 | lifeskim:mentions | umls-concept:C0086376 | lld:lifeskim |
| pubmed-article:15086781 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:15086781 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:15086781 | lifeskim:mentions | umls-concept:C1705944 | lld:lifeskim |
| pubmed-article:15086781 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:15086781 | lifeskim:mentions | umls-concept:C1522408 | lld:lifeskim |
| pubmed-article:15086781 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:15086781 | lifeskim:mentions | umls-concept:C0453946 | lld:lifeskim |
| pubmed-article:15086781 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:15086781 | pubmed:dateCreated | 2004-4-16 | lld:pubmed |
| pubmed-article:15086781 | pubmed:abstractText | The trans-Golgi network is the major sorting compartment of the secretory pathway for protein, lipid and membrane traffic. There is a constant flow of membrane and cargo to and from this compartment. Evidence is emerging that the trans-Golgi network has multiple biochemically and functionally distinct subdomains, each of which contributes to the combined sorting and transport requirements of this dynamic compartment. The recruitment of distinct arrays of protein complexes to trans-Golgi network membranes is likely to produce the diversity of structure and biochemistry observed amongst subdomains that serve to generate different carriers or maintain resident trans-Golgi network components. This review discusses how these subdomains may be formed and examines the molecular players involved, including G proteins, clathrin adaptors and golgin tethers. Diversity within these protein families is highlighted and shown to be critical for the functionality of the trans-Golgi network, as a mediator of protein sorting and membrane transport, and for the maintenance of Golgi structure. | lld:pubmed |
| pubmed-article:15086781 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15086781 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15086781 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15086781 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:15086781 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15086781 | pubmed:month | May | lld:pubmed |
| pubmed-article:15086781 | pubmed:issn | 1398-9219 | lld:pubmed |
| pubmed-article:15086781 | pubmed:author | pubmed-author:GleesonPaul... | lld:pubmed |
| pubmed-article:15086781 | pubmed:author | pubmed-author:StowJennifer... | lld:pubmed |
| pubmed-article:15086781 | pubmed:author | pubmed-author:LukeMichael... | lld:pubmed |
| pubmed-article:15086781 | pubmed:author | pubmed-author:LockJohn GJG | lld:pubmed |
| pubmed-article:15086781 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15086781 | pubmed:volume | 5 | lld:pubmed |
| pubmed-article:15086781 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15086781 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15086781 | pubmed:pagination | 315-26 | lld:pubmed |
| pubmed-article:15086781 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:15086781 | pubmed:meshHeading | pubmed-meshheading:15086781... | lld:pubmed |
| pubmed-article:15086781 | pubmed:meshHeading | pubmed-meshheading:15086781... | lld:pubmed |
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| pubmed-article:15086781 | pubmed:meshHeading | pubmed-meshheading:15086781... | lld:pubmed |
| pubmed-article:15086781 | pubmed:meshHeading | pubmed-meshheading:15086781... | lld:pubmed |
| pubmed-article:15086781 | pubmed:meshHeading | pubmed-meshheading:15086781... | lld:pubmed |
| pubmed-article:15086781 | pubmed:meshHeading | pubmed-meshheading:15086781... | lld:pubmed |
| pubmed-article:15086781 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15086781 | pubmed:articleTitle | Domains of the TGN: coats, tethers and G proteins. | lld:pubmed |
| pubmed-article:15086781 | pubmed:affiliation | The Russell Grimwade School of Biochemistry and Molecular Biology, The University of Melbourne, Melbourne, Victoria 3010, Australia. pgleeson@unimelb.edu.au | lld:pubmed |
| pubmed-article:15086781 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15086781 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:15086781 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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