| pubmed-article:15466472 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15466472 | lifeskim:mentions | umls-concept:C0521390 | lld:lifeskim |
| pubmed-article:15466472 | lifeskim:mentions | umls-concept:C0077678 | lld:lifeskim |
| pubmed-article:15466472 | lifeskim:mentions | umls-concept:C0132555 | lld:lifeskim |
| pubmed-article:15466472 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:15466472 | lifeskim:mentions | umls-concept:C1420492 | lld:lifeskim |
| pubmed-article:15466472 | lifeskim:mentions | umls-concept:C0600596 | lld:lifeskim |
| pubmed-article:15466472 | lifeskim:mentions | umls-concept:C0057856 | lld:lifeskim |
| pubmed-article:15466472 | pubmed:issue | 51 | lld:pubmed |
| pubmed-article:15466472 | pubmed:dateCreated | 2004-12-13 | lld:pubmed |
| pubmed-article:15466472 | pubmed:abstractText | It is established that neuronal nitric-oxide synthase (nNOS) is ubiquitylated and proteasomally degraded. The proteasomal degradation of nNOS is enhanced by suicide inactivation of nNOS or by the inhibition of hsp90, which is a chaperone found in a native complex with nNOS. In the current study, we have examined whether CHIP, a chaperone-dependent E3 ubiquitin-protein isopeptide ligase that is known to ubiquitylate other hsp90-chaperoned proteins, could act as an ubiquitin ligase for nNOS. We found with the use of HEK293T or COS-7 cells and transient transfection methods that CHIP overexpression causes a decrease in immunodetectable levels of nNOS. The extent of the loss of nNOS is dependent on the amount of CHIP cDNA used for transfection. Lactacystin (10 microM), a selective proteasome inhibitor, attenuates the loss of nNOS in part by causing the nNOS to be found in a detergent-insoluble form. Immunoprecipitation of the nNOS and subsequent Western blotting with an anti-ubiquitin IgG shows an increase in nNOS-ubiquitin conjugates because of CHIP. Moreover, incubation of nNOS with a purified system containing an E1 ubiquitin-activating enzyme, an E2 ubiquitin carrier protein conjugating enzyme (UbcH5a), CHIP, glutathione S-transferase-tagged ubiquitin, and an ATP-generating system leads to the ubiquitylation of nNOS. The addition of purified hsp70 and hsp40 to this in vitro system greatly enhances the amount of nNOS-ubiquitin conjugates, suggesting that CHIP is an E3 ligase for nNOS whose action is facilitated by (and possibly requires) its interaction with nNOS-bound hsp70. | lld:pubmed |
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| pubmed-article:15466472 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15466472 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15466472 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15466472 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:15466472 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15466472 | pubmed:author | pubmed-author:PattersonCamC | lld:pubmed |
| pubmed-article:15466472 | pubmed:author | pubmed-author:PrattWilliam... | lld:pubmed |
| pubmed-article:15466472 | pubmed:author | pubmed-author:OsawaYoichiY | lld:pubmed |
| pubmed-article:15466472 | pubmed:author | pubmed-author:LauMirandaM | lld:pubmed |
| pubmed-article:15466472 | pubmed:author | pubmed-author:PengHwei-Ming... | lld:pubmed |
| pubmed-article:15466472 | pubmed:author | pubmed-author:MorishimaYosh... | lld:pubmed |
| pubmed-article:15466472 | pubmed:author | pubmed-author:DunbarAnwar... | lld:pubmed |
| pubmed-article:15466472 | pubmed:author | pubmed-author:JenkinsGary... | lld:pubmed |
| pubmed-article:15466472 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15466472 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:15466472 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:15466472 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15466472 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15466472 | pubmed:pagination | 52970-7 | lld:pubmed |
| pubmed-article:15466472 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:15466472 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15466472 | pubmed:articleTitle | Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase. | lld:pubmed |
| pubmed-article:15466472 | pubmed:affiliation | Department of Pharmacology, University of Michigan Medical School, Ann Arbor, MI 48109, USA. | lld:pubmed |
| pubmed-article:15466472 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15466472 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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