| pubmed-article:8262066 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:8262066 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:8262066 | lifeskim:mentions | umls-concept:C1326243 | lld:lifeskim |
| pubmed-article:8262066 | lifeskim:mentions | umls-concept:C1705248 | lld:lifeskim |
| pubmed-article:8262066 | lifeskim:mentions | umls-concept:C1548799 | lld:lifeskim |
| pubmed-article:8262066 | lifeskim:mentions | umls-concept:C1524073 | lld:lifeskim |
| pubmed-article:8262066 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:8262066 | lifeskim:mentions | umls-concept:C0449432 | lld:lifeskim |
| pubmed-article:8262066 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:8262066 | pubmed:dateCreated | 1994-1-26 | lld:pubmed |
| pubmed-article:8262066 | pubmed:abstractText | The beta 1 and beta 2 subunits are the closely-related large chains of the trans-Golgi network AP-1 and the plasma membrane AP-2 clathrin-associated protein complexes, respectively. Recombinant beta 1 and beta 2 subunits have been generated in Escherichia coli. It was found that, in the absence of all the other AP subunits, beta 1 and beta 2 interact with clathrin and drive the efficient assembly of clathrin coats. In addition, beta 2 subunits and AP complexes compete for the same clathrin binding site. The appearance of the clathrin/beta coats is the same as the barrel-shaped structures formed with native AP complexes. It is proposed that the principal function of the beta subunits is to initiate coat formation, while the remaining subunits of the AP complexes have other roles in coated pit and coated vesicle function. | lld:pubmed |
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| pubmed-article:8262066 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8262066 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8262066 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8262066 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8262066 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:8262066 | pubmed:author | pubmed-author:KirchhausenTT | lld:pubmed |
| pubmed-article:8262066 | pubmed:author | pubmed-author:GallusserAA | lld:pubmed |
| pubmed-article:8262066 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8262066 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8262066 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:8262066 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8262066 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8262066 | pubmed:pagination | 5237-44 | lld:pubmed |
| pubmed-article:8262066 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8262066 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8262066 | pubmed:articleTitle | The beta 1 and beta 2 subunits of the AP complexes are the clathrin coat assembly components. | lld:pubmed |
| pubmed-article:8262066 | pubmed:affiliation | Harvard Medical School, Department of Cell Biology, Boston, MA 02115. | lld:pubmed |
| pubmed-article:8262066 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8262066 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8262066 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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