| pubmed-article:1924354 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1924354 | lifeskim:mentions | umls-concept:C0002520 | lld:lifeskim |
| pubmed-article:1924354 | lifeskim:mentions | umls-concept:C0288472 | lld:lifeskim |
| pubmed-article:1924354 | lifeskim:mentions | umls-concept:C0249197 | lld:lifeskim |
| pubmed-article:1924354 | lifeskim:mentions | umls-concept:C0033666 | lld:lifeskim |
| pubmed-article:1924354 | lifeskim:mentions | umls-concept:C1420626 | lld:lifeskim |
| pubmed-article:1924354 | lifeskim:mentions | umls-concept:C0682996 | lld:lifeskim |
| pubmed-article:1924354 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:1924354 | pubmed:dateCreated | 1991-11-15 | lld:pubmed |
| pubmed-article:1924354 | pubmed:abstractText | ras proteins undergo posttranslational modification by a 15-carbon farnesyl isoprenoid at a cysteine within a defined COOH-terminal amino acid motif; i.e., Cys-Ali-Ali-Ser/Met (where Ali represents an aliphatic residue). In other low molecular mass GTP-binding proteins, cysteines are modified by 20-carbon geranylgeranyl groups within a Cys-Ali-Ali-Leu motif. We changed the terminal Ser-189 of Ha-ras p21 to Leu-189 by site-directed mutagenesis and found that the protein was modified by [3H]geranylgeranyl instead of [3H]farnesyl in an in vitro assay. Gel-permeation chromatography of [3H]mevalonate-labeled hydrocarbons released from immunoprecipitated ras proteins overexpressed in COS cells indicated that Ha-ras p21(Leu-189) was also a substrate for 20-carbon isoprenyl modification in vivo. Additional steps in Ha-ras p21 processing, normally initiated by farnesylation, appear to be supported by geranylgeranylation, based on metabolic labeling of Ha-ras p21(Leu-189) with [3H]palmitate and its subcellular localization in a particulate fraction from COS cells. These observations indicate that the amino acid occupying the terminal position (Xaa) in the Cys-Ali-Ali-Xaa motif constitutes a key structural feature by which Ha-ras p21 and other proteins with ras-like COOH-terminal isoprenylation sites are distinguished as substrates for farnesyl- or geranylgeranyltransferases. | lld:pubmed |
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| pubmed-article:1924354 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1924354 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1924354 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1924354 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1924354 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:1924354 | pubmed:author | pubmed-author:MalteseW AWA | lld:pubmed |
| pubmed-article:1924354 | pubmed:author | pubmed-author:ErdmanR ARA | lld:pubmed |
| pubmed-article:1924354 | pubmed:author | pubmed-author:KinsellaB TBT | lld:pubmed |
| pubmed-article:1924354 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1924354 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:1924354 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:1924354 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1924354 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1924354 | pubmed:pagination | 8934-8 | lld:pubmed |
| pubmed-article:1924354 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:1924354 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1924354 | pubmed:articleTitle | Posttranslational modification of Ha-ras p21 by farnesyl versus geranylgeranyl isoprenoids is determined by the COOH-terminal amino acid. | lld:pubmed |
| pubmed-article:1924354 | pubmed:affiliation | Weis Center for Research, Geisinger Clinic, Danville, PA 17822. | lld:pubmed |
| pubmed-article:1924354 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1924354 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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