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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2009-2-9
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pubmed:abstractText |
Viperin is an evolutionarily conserved interferon-inducible protein that localizes to the endoplasmic reticulum (ER) and inhibits a number of DNA and RNA viruses. In this study, we report that viperin specifically localizes to the cytoplasmic face of the ER and that an amphipathic alpha-helix at its N terminus is necessary for the ER localization of viperin and sufficient to promote ER localization of a reporter protein, dsRed. Overexpression of intact viperin but not the amphipathic alpha-helix fused to dsRed induced crystalloid ER. Consistent with other proteins that induce crystalloid ER, viperin self-associates, and it does so independently of the amphipathic alpha-helix. Viperin expression also affected the transport of soluble but not membrane-associated proteins. Expression of intact viperin or an N-terminal alpha-helix-dsRed fusion protein significantly reduced secretion of soluble alkaline phosphatase and reduced its rate of ER-to-Golgi trafficking. Similarly, viperin expression inhibited bulk protein secretion and secretion of endogenous alpha(1)-antitrypsin and serum albumin from HepG2 cells. Converting hydrophobic residues in the N-terminal alpha-helix to acidic residues partially or completely restored normal transport of soluble alkaline phosphatase, suggesting that the extended amphipathic nature of the N-terminal alpha-helical domain is essential for inhibiting protein secretion.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-11533032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-11752458,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-11780124,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-12209136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-14581454,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-14581457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-15252131,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-16108059,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-16122427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-16190978,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-16193070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-16319878,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-16364743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-16365634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-16782321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-16982913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-17686841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-18005724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-18077728,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-18414501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-3417148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-6705048,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-8288610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-8832395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19074433-9288971
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4705-12
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:19074433-DNA Viruses,
pubmed-meshheading:19074433-Endoplasmic Reticulum,
pubmed-meshheading:19074433-Golgi Apparatus,
pubmed-meshheading:19074433-HeLa Cells,
pubmed-meshheading:19074433-Humans,
pubmed-meshheading:19074433-Protein Structure, Secondary,
pubmed-meshheading:19074433-Protein Structure, Tertiary,
pubmed-meshheading:19074433-Protein Transport,
pubmed-meshheading:19074433-Proteins,
pubmed-meshheading:19074433-RNA Viruses,
pubmed-meshheading:19074433-Serum Albumin,
pubmed-meshheading:19074433-alpha 1-Antitrypsin
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pubmed:year |
2009
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pubmed:articleTitle |
The N-terminal amphipathic alpha-helix of viperin mediates localization to the cytosolic face of the endoplasmic reticulum and inhibits protein secretion.
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pubmed:affiliation |
Section of Microbial Pathogenesis, Yale University School of Medicine, New Haven, Connecticut 06520-8011, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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