pubmed-article:18451503 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:18451503 | lifeskim:mentions | umls-concept:C1327616 | lld:lifeskim |
pubmed-article:18451503 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:18451503 | lifeskim:mentions | umls-concept:C1516451 | lld:lifeskim |
pubmed-article:18451503 | lifeskim:mentions | umls-concept:C1514623 | lld:lifeskim |
pubmed-article:18451503 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:18451503 | pubmed:dateCreated | 2008-5-2 | lld:pubmed |
pubmed-article:18451503 | pubmed:abstractText | Small ubiquitin-related modifier (SUMO) is a type I ubiquitin-like protein family member and is covalently attached to various target proteins. Through this post-translational modification, SUMO plays important roles in various cellular events. Here, we show that SUMO is secreted from cultured cells in an endoplasmic reticulum (ER)/Golgi-independent manner and that this secretion occurs without covalent binding to target proteins or chain formation. Overexpression experiments using C-terminally truncated mutants of SUMO revealed that the secretion requires the C-terminal sequence. Recombinant SUMO-3 protein was capable of binding to and promoting the proliferation of cultured cells. Thus, we propose that SUMO functions as a cytokine-like molecule extracellularly. | lld:pubmed |
pubmed-article:18451503 | pubmed:language | eng | lld:pubmed |
pubmed-article:18451503 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18451503 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:18451503 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18451503 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18451503 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18451503 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18451503 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:18451503 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:18451503 | pubmed:month | May | lld:pubmed |
pubmed-article:18451503 | pubmed:issn | 0918-6158 | lld:pubmed |
pubmed-article:18451503 | pubmed:author | pubmed-author:YokosawaHidey... | lld:pubmed |
pubmed-article:18451503 | pubmed:author | pubmed-author:HosonoHidetak... | lld:pubmed |
pubmed-article:18451503 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:18451503 | pubmed:volume | 31 | lld:pubmed |
pubmed-article:18451503 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:18451503 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:18451503 | pubmed:pagination | 834-7 | lld:pubmed |
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pubmed-article:18451503 | pubmed:year | 2008 | lld:pubmed |
pubmed-article:18451503 | pubmed:articleTitle | Small ubiquitin-related modifier is secreted and shows cytokine-like activity. | lld:pubmed |
pubmed-article:18451503 | pubmed:affiliation | Department of Biochemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan. | lld:pubmed |
pubmed-article:18451503 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:18451503 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |