| pubmed-article:7797559 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7797559 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:7797559 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:7797559 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:7797559 | lifeskim:mentions | umls-concept:C0024742 | lld:lifeskim |
| pubmed-article:7797559 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:7797559 | lifeskim:mentions | umls-concept:C0084175 | lld:lifeskim |
| pubmed-article:7797559 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:7797559 | pubmed:dateCreated | 1995-8-1 | lld:pubmed |
| pubmed-article:7797559 | pubmed:abstractText | The recognition of lysosomal enzymes by UDP-GlcNAc: lysosomal-enzyme GlcNAc-1-phosphotransferase (phosphotransferase) is mediated by a protein structure on lysosomal enzymes. It has been previously demonstrated that lysine residues are required for phosphorylation of procathepsin L and are a common feature of the site on many lysosomal proteins. In this work, the procathepsin L recognition structure was further defined by identification of the region of the protein containing the structure and the critical lysine residues involved. Removal of the cathepsin L propeptide by low pH-induced autocatalytic processing abolished phosphorylation. The addition of either the purified propeptide or a glutathione S-transferase-propeptide fusion protein to the processed protein restored phosphorylation. Mutagenesis of individual lysine residues demonstrated that two propeptide lysine residues (Lys-54 and Lys-99) were required for efficient phosphorylation of procathepsin L. By comparison of the phosphorylation rates of procathepsin L, lysine-modified procathepsin L, and the procathepsin L oligosaccharide, lysine residues were shown to account for most, if not all, of the protein-dependent interaction. On this basis, it is concluded that the proregion lysine residues are the major elements of the procathepsin L recognition site. In addition, lysine residues in cathepsin D were shown to be as important for phosphorylation as those in procathepsin L, supporting a general model of the recognition site as a specific three-dimensional arrangement of lysine residues exposed on the surface of lysosomal proteins. | lld:pubmed |
| pubmed-article:7797559 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797559 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7797559 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797559 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7797559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797559 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7797559 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7797559 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7797559 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7797559 | pubmed:author | pubmed-author:SahagianG GGG | lld:pubmed |
| pubmed-article:7797559 | pubmed:author | pubmed-author:TapJJ | lld:pubmed |
| pubmed-article:7797559 | pubmed:author | pubmed-author:YoungWW | lld:pubmed |
| pubmed-article:7797559 | pubmed:author | pubmed-author:CuozzoJ WJW | lld:pubmed |
| pubmed-article:7797559 | pubmed:author | pubmed-author:WuQ LQL | lld:pubmed |
| pubmed-article:7797559 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7797559 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:7797559 | pubmed:volume | 270 | lld:pubmed |
| pubmed-article:7797559 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7797559 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7797559 | pubmed:pagination | 15611-9 | lld:pubmed |
| pubmed-article:7797559 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:7797559 | pubmed:meshHeading | pubmed-meshheading:7797559-... | lld:pubmed |
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| pubmed-article:7797559 | pubmed:meshHeading | pubmed-meshheading:7797559-... | lld:pubmed |
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| pubmed-article:7797559 | pubmed:meshHeading | pubmed-meshheading:7797559-... | lld:pubmed |
| pubmed-article:7797559 | pubmed:meshHeading | pubmed-meshheading:7797559-... | lld:pubmed |
| pubmed-article:7797559 | pubmed:meshHeading | pubmed-meshheading:7797559-... | lld:pubmed |
| pubmed-article:7797559 | pubmed:meshHeading | pubmed-meshheading:7797559-... | lld:pubmed |
| pubmed-article:7797559 | pubmed:meshHeading | pubmed-meshheading:7797559-... | lld:pubmed |
| pubmed-article:7797559 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7797559 | pubmed:articleTitle | Lysine-based structure in the proregion of procathepsin L is the recognition site for mannose phosphorylation. | lld:pubmed |
| pubmed-article:7797559 | pubmed:affiliation | Department of Physiology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA. | lld:pubmed |
| pubmed-article:7797559 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7797559 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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