| pubmed-article:9724753 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9724753 | lifeskim:mentions | umls-concept:C0035499 | lld:lifeskim |
| pubmed-article:9724753 | lifeskim:mentions | umls-concept:C1519249 | lld:lifeskim |
| pubmed-article:9724753 | lifeskim:mentions | umls-concept:C0599896 | lld:lifeskim |
| pubmed-article:9724753 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:9724753 | lifeskim:mentions | umls-concept:C1947906 | lld:lifeskim |
| pubmed-article:9724753 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:9724753 | pubmed:issue | 18 | lld:pubmed |
| pubmed-article:9724753 | pubmed:dateCreated | 1998-9-28 | lld:pubmed |
| pubmed-article:9724753 | pubmed:abstractText | Several mutations that cause severe forms of the human disease autosomal dominant retinitis pigmentosa cluster in the C-terminal region of rhodopsin. Recent studies have implicated the C-terminal domain of rhodopsin in its trafficking on specialized post-Golgi membranes to the rod outer segment of the photoreceptor cell. Here we used synthetic peptides as competitive inhibitors of rhodopsin trafficking in the frog retinal cell-free system to delineate the potential regulatory sequence within the C terminus of rhodopsin and model the effects of severe retinitis pigmentosa alleles on rhodopsin sorting. The rhodopsin C-terminal sequence QVS(A)PA is highly conserved among different species. Peptides that correspond to the C terminus of bovine (amino acids 324-348) and frog (amino acids 330-354) rhodopsin inhibited post-Golgi trafficking by 50% and 60%, respectively, and arrested newly synthesized rhodopsin in the trans-Golgi network. Peptides corresponding to the cytoplasmic loops of rhodopsin and other control peptides had no effect. When three naturally occurring mutations: Q344ter (lacking the last five amino acids QVAPA), V345M, and P347S were introduced into the frog C-terminal peptide, the inhibitory activity of the peptides was no longer detectable. These observations suggest that the amino acids QVS(A)PA comprise a signal that is recognized by specific factors in the trans-Golgi network. A lack of recognition of this sequence, because of mutations in the last five amino acids causing autosomal dominant retinitis pigmentosa, most likely results in abnormal post-Golgi membrane formation and in an aberrant subcellular localization of rhodopsin. | lld:pubmed |
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| pubmed-article:9724753 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9724753 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9724753 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9724753 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9724753 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9724753 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:9724753 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:9724753 | pubmed:author | pubmed-author:HargraveP APA | lld:pubmed |
| pubmed-article:9724753 | pubmed:author | pubmed-author:McDowellJ HJH | lld:pubmed |
| pubmed-article:9724753 | pubmed:author | pubmed-author:ArendtAA | lld:pubmed |
| pubmed-article:9724753 | pubmed:author | pubmed-author:DereticDD | lld:pubmed |
| pubmed-article:9724753 | pubmed:author | pubmed-author:SchmerlSS | lld:pubmed |
| pubmed-article:9724753 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9724753 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9724753 | pubmed:volume | 95 | lld:pubmed |
| pubmed-article:9724753 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9724753 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9724753 | pubmed:pagination | 10620-5 | lld:pubmed |
| pubmed-article:9724753 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9724753 | pubmed:meshHeading | pubmed-meshheading:9724753-... | lld:pubmed |
| pubmed-article:9724753 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9724753 | pubmed:articleTitle | Regulation of sorting and post-Golgi trafficking of rhodopsin by its C-terminal sequence QVS(A)PA. | lld:pubmed |
| pubmed-article:9724753 | pubmed:affiliation | Department of Ophthalmology, University of Michigan, Ann Arbor, MI 48105, USA. dereticd@umich.edu | lld:pubmed |
| pubmed-article:9724753 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9724753 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9724753 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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