| pubmed-article:9382861 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9382861 | lifeskim:mentions | umls-concept:C0034861 | lld:lifeskim |
| pubmed-article:9382861 | lifeskim:mentions | umls-concept:C0021699 | lld:lifeskim |
| pubmed-article:9382861 | lifeskim:mentions | umls-concept:C0599895 | lld:lifeskim |
| pubmed-article:9382861 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:9382861 | lifeskim:mentions | umls-concept:C0138903 | lld:lifeskim |
| pubmed-article:9382861 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9382861 | pubmed:dateCreated | 1997-12-30 | lld:pubmed |
| pubmed-article:9382861 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9382861 | pubmed:abstractText | Here, we report the localization and characterization of BHKp23, a member of the p24 family of transmembrane proteins, in mammalian cells. We find that p23 is a major component of tubulovesicular membranes at the cis side of the Golgi complex (estimated density: 12,500 copies/micron2 membrane surface area, or approximately 30% of the total protein). Our data indicate that BHKp23-containing membranes are part of the cis-Golgi network/intermediate compartment. Using the G protein of vesicular stomatitis virus as a transmembrane cargo molecule, we find that p23 membranes are an obligatory station in forward biosynthetic membrane transport, but that p23 itself is absent from transport vesicles that carry the G protein to and beyond the Golgi complex. Our data show that p23 is not present to any significant extent in coat protein (COP) I-coated vesicles generated in vitro and does not colocalize with COP I buds and vesicles. Moreover, we find that p23 cytoplasmic domain is not involved in COP I membrane recruitment. Our data demonstrate that microinjected antibodies against the cytoplasmic tail of p23 inhibit G protein transport from the cis-Golgi network/ intermediate compartment to the cell surface, suggesting that p23 function is required for the transport of transmembrane cargo molecules. These observations together with the fact that p23 is a highly abundant component in the intermediate compartment, lead us to propose that p23 contributes to membrane structure, and that this contribution is necessary for efficient segregation and transport. | lld:pubmed |
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| pubmed-article:9382861 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9382861 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9382861 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9382861 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9382861 | pubmed:month | Dec | lld:pubmed |
