| pubmed-article:12535272 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12535272 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:12535272 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:12535272 | lifeskim:mentions | umls-concept:C0024742 | lld:lifeskim |
| pubmed-article:12535272 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:12535272 | lifeskim:mentions | umls-concept:C1424620 | lld:lifeskim |
| pubmed-article:12535272 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:12535272 | pubmed:dateCreated | 2003-1-21 | lld:pubmed |
| pubmed-article:12535272 | pubmed:abstractText | TIP47 (tail-interacting protein of 47 kDa) binds to the cytoplasmic domains of mannose 6-phosphate receptors and is required for their transport from endosomes to the trans-Golgi network in vitro and in living cells. TIP47 occurs in cytosol as an oligomer; it chromatographs with an apparent mass of approximately 300 kDa and displays an S-value of approximately 13. Recombinant TIP47 forms homo-oligomers that are likely to represent hexamers, as determined by chemical cross-linking. Removal of TIP47 residues 1-151 yields a protein that behaves as a monomer upon gel filtration, yet is fully capable of binding mannose 6-phosphate receptor cytoplasmic domains. The presence of an oligomerization domain in the N-terminus of TIP47 was confirmed by expression of N-terminal residues 1-133 or 1-257 in mammalian cells. Co-expression of full-length TIP47 with either of these fragments led to the formation of higher-order aggregates of wild-type TIP47. Furthermore, the N-terminal domains expressed alone also occurred as oligomers. These studies reveal an N-terminal oligomerization domain in TIP47, and show that oligomerization is not required for TIP47 recognition of mannose 6-phosphate receptors. However, oligomerization is required for TIP47 stimulation of mannose 6-phosphate receptor transport from endosomes to the trans-Golgi in vivo. | lld:pubmed |
| pubmed-article:12535272 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12535272 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12535272 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12535272 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12535272 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12535272 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12535272 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12535272 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12535272 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:12535272 | pubmed:issn | 1398-9219 | lld:pubmed |
| pubmed-article:12535272 | pubmed:author | pubmed-author:PfefferSuzann... | lld:pubmed |
| pubmed-article:12535272 | pubmed:author | pubmed-author:SivarsUlfU | lld:pubmed |
| pubmed-article:12535272 | pubmed:author | pubmed-author:DingLiL | lld:pubmed |
| pubmed-article:12535272 | pubmed:author | pubmed-author:O'ConnorBrian... | lld:pubmed |
| pubmed-article:12535272 | pubmed:author | pubmed-author:DiederichsSve... | lld:pubmed |
| pubmed-article:12535272 | pubmed:author | pubmed-author:SincockPaul... | lld:pubmed |
| pubmed-article:12535272 | pubmed:author | pubmed-author:GanleyIan GIG | lld:pubmed |
| pubmed-article:12535272 | pubmed:author | pubmed-author:KriseJeffrey... | lld:pubmed |
| pubmed-article:12535272 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12535272 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:12535272 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12535272 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12535272 | pubmed:pagination | 18-25 | lld:pubmed |
| pubmed-article:12535272 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:12535272 | pubmed:meshHeading | pubmed-meshheading:12535272... | lld:pubmed |
| pubmed-article:12535272 | pubmed:meshHeading | pubmed-meshheading:12535272... | lld:pubmed |
| pubmed-article:12535272 | pubmed:meshHeading | pubmed-meshheading:12535272... | lld:pubmed |
| pubmed-article:12535272 | pubmed:meshHeading | pubmed-meshheading:12535272... | lld:pubmed |
| pubmed-article:12535272 | pubmed:meshHeading | pubmed-meshheading:12535272... | lld:pubmed |
| pubmed-article:12535272 | pubmed:meshHeading | pubmed-meshheading:12535272... | lld:pubmed |
| pubmed-article:12535272 | pubmed:meshHeading | pubmed-meshheading:12535272... | lld:pubmed |
| pubmed-article:12535272 | pubmed:meshHeading | pubmed-meshheading:12535272... | lld:pubmed |
| pubmed-article:12535272 | pubmed:meshHeading | pubmed-meshheading:12535272... | lld:pubmed |
| pubmed-article:12535272 | pubmed:meshHeading | pubmed-meshheading:12535272... | lld:pubmed |
| pubmed-article:12535272 | pubmed:meshHeading | pubmed-meshheading:12535272... | lld:pubmed |
| pubmed-article:12535272 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12535272 | pubmed:articleTitle | Self-assembly is important for TIP47 function in mannose 6-phosphate receptor transport. | lld:pubmed |
| pubmed-article:12535272 | pubmed:affiliation | Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA. | lld:pubmed |
| pubmed-article:12535272 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12535272 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12535272 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:10226 | entrezgene:pubmed | pubmed-article:12535272 | lld:entrezgene |
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