rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
5
|
pubmed:dateCreated |
2008-5-2
|
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.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0918-6158
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
31
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
834-7
|
pubmed:meshHeading |
pubmed-meshheading:18451503-Animals,
pubmed-meshheading:18451503-Antibodies, Blocking,
pubmed-meshheading:18451503-Blotting, Western,
pubmed-meshheading:18451503-Brefeldin A,
pubmed-meshheading:18451503-Cell Proliferation,
pubmed-meshheading:18451503-Cells, Cultured,
pubmed-meshheading:18451503-Cytokines,
pubmed-meshheading:18451503-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:18451503-Endoplasmic Reticulum,
pubmed-meshheading:18451503-HeLa Cells,
pubmed-meshheading:18451503-Humans,
pubmed-meshheading:18451503-Mice,
pubmed-meshheading:18451503-NIH 3T3 Cells,
pubmed-meshheading:18451503-Plasmids,
pubmed-meshheading:18451503-Recombinant Proteins,
pubmed-meshheading:18451503-Small Ubiquitin-Related Modifier Proteins
|
pubmed:year |
2008
|
pubmed:articleTitle |
Small ubiquitin-related modifier is secreted and shows cytokine-like activity.
|
pubmed:affiliation |
Department of Biochemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|