Linked Life Data

19561072

Source:http://linkedlifedata.com/resource/pubmed/id/19561072

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
2009-8-31
pubmed:abstractText
Co-translational import into the endoplasmic reticulum (ER) is primarily controlled by N-terminal signal sequences that mediate targeting of the ribosome-nascent chain complex to the Sec61/translocon and initiate the translocation process. Here we show that after targeting to the translocon the secondary structure of the nascent polypeptide chain can significantly modulate translocation efficiency. ER-targeted polypeptides dominated by unstructured domains failed to efficiently translocate into the ER lumen and were subjected to proteasomal degradation via a co-translocational/preemptive pathway. Productive ER import could be reinstated by increasing the amount of alpha-helical domains, whereas more effective ER signal sequences had only a minor effect on ER import efficiency of unstructured polypeptides. ER stress and overexpression of p58(IPK) promoted the co-translocational degradation pathway. Moreover polypeptides with unstructured domains at their N terminus were specifically targeted to proteasomal degradation under these conditions. Our study indicates that extended unstructured domains are signals to dispose ER-targeted proteins via a co-translocational, preemptive quality control pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
284
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
24384-93
pubmed:dateRevised
2010-9-7
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
alpha-Helical domains promote translocation of intrinsically disordered polypeptides into the endoplasmic reticulum.
pubmed:affiliation
Neurobiochemistry, Deutsches Zentrum für Neurodegenerative Erkrankungen and Adolf-Butenandt-Institut, Ludwig-Maximilians-Universität München, D-80336 München, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't