| pubmed-article:20959456 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20959456 | lifeskim:mentions | umls-concept:C0285890 | lld:lifeskim |
| pubmed-article:20959456 | lifeskim:mentions | umls-concept:C1752727 | lld:lifeskim |
| pubmed-article:20959456 | lifeskim:mentions | umls-concept:C0599894 | lld:lifeskim |
| pubmed-article:20959456 | lifeskim:mentions | umls-concept:C1521840 | lld:lifeskim |
| pubmed-article:20959456 | pubmed:issue | 52 | lld:pubmed |
| pubmed-article:20959456 | pubmed:dateCreated | 2010-12-20 | lld:pubmed |
| pubmed-article:20959456 | pubmed:abstractText | ?-Synuclein (a-Syn) is a major component of fibrillar aggregates in Lewy bodies (LBs), a characteristic hallmark of Parkinson disease. Almost 90% of a-Syn deposited in LBs is phosphorylated at Ser-129. However, the role of Ser-129-phosphorylated a-Syn in the biogenesis of LBs remains unclear. Here, we investigated the metabolism of Ser-129-phosphorylated a-Syn. In SH-SY5Y cells, inhibition of protein phosphatase 2A/1 by okadaic acid, and inhibition of the proteasome pathway by MG132 or lactacystin accumulated Ser-129-phosphorylated a-Syn. However, these inhibitions did not alter the amounts of total a-Syn within the observation time. Inhibition of the autophagy-lysosome pathway by 3-methyladenine or chloroquine accumulated Ser-129-phosphorylated a-Syn in parallel to total a-Syn during longer incubations. Experiments using cycloheximide showed that Ser-129-phosphorylated a-Syn diminished rapidly (t(½) = 54.9 ± 6.4 min), in contrast to the stably expressed total a-Syn. The short half-life of Ser-129-phosphorylated a-Syn was blocked by MG132 to a greater extent than okadaic acid. In rat primary cortical neurons, either MG132, lactacystin, or okadaic acid accumulated Ser-129-phosphorylated a-Syn. Additionally, we did not find that phosphorylated a-Syn was ubiquitinated in the presence of proteasome inhibitors. These data show that Ser-129-phosphorylated a-Syn is targeted to the proteasome pathway in a ubiquitin-independent manner, in addition to undergoing dephosphorylation. The proteasome pathway may play a role in the biogenesis of Ser-129-phosphorylated a-Syn-rich LBs. | lld:pubmed |
| pubmed-article:20959456 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20959456 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20959456 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20959456 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:20959456 | pubmed:issn | 1083-351X | lld:pubmed |
| pubmed-article:20959456 | pubmed:author | pubmed-author:SatoHiroyasuH | lld:pubmed |
| pubmed-article:20959456 | pubmed:author | pubmed-author:KatoTakeoT | lld:pubmed |
| pubmed-article:20959456 | pubmed:author | pubmed-author:SakamotoMasah... | lld:pubmed |
| pubmed-article:20959456 | pubmed:author | pubmed-author:ArawakaShigek... | lld:pubmed |
| pubmed-article:20959456 | pubmed:author | pubmed-author:KoyamaShingoS | lld:pubmed |
| pubmed-article:20959456 | pubmed:author | pubmed-author:HaraSusumuS | lld:pubmed |
| pubmed-article:20959456 | pubmed:author | pubmed-author:MachiyaYouhei... | lld:pubmed |
| pubmed-article:20959456 | pubmed:author | pubmed-author:FukushimaShin... | lld:pubmed |
| pubmed-article:20959456 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20959456 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:20959456 | pubmed:volume | 285 | lld:pubmed |
| pubmed-article:20959456 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20959456 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20959456 | pubmed:pagination | 40732-44 | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:meshHeading | pubmed-meshheading:20959456... | lld:pubmed |
| pubmed-article:20959456 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20959456 | pubmed:articleTitle | Phosphorylated alpha-synuclein at Ser-129 is targeted to the proteasome pathway in a ubiquitin-independent manner. | lld:pubmed |
| pubmed-article:20959456 | pubmed:affiliation | Department of Neurology, Hematology, Metabolism, Endocrinology, and Diabetology, Faculty of Medicine, Yamagata University, Yamagata 990-9585, Japan. | lld:pubmed |
| pubmed-article:20959456 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20959456 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:6622 | entrezgene:pubmed | pubmed-article:20959456 | lld:entrezgene |
| entrez-gene:29219 | entrezgene:pubmed | pubmed-article:20959456 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20959456 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:20959456 | lld:entrezgene |
