Linked Life Data

9409541

Source:http://linkedlifedata.com/resource/pubmed/id/9409541

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1998-1-15
pubmed:abstractText
The endoplasmic reticulum (ER) is the site of entry of proteins into the secretory pathway. It is responsible for proper folding of the proteins before delivery to their site of action. Furthermore, proofreading to detect malfolded or unnecessary proteins that have to be eliminated and regulation of protein levels are crucial ER functions. The ubiquitin-proteasome system, located in the cytoplasm, has emerged as the major ER degradation machinery. A multitude of ER resident as well as membrane-bound and soluble proteolytic substrates of the secretory pathway are retained in the ER and destined for degradation via this pathway. Their actual proteolysis is preceded by a retrograde transport to the cytoplasm. A key component of the translocation apparatus, Sec61p, is also the central subunit of the retrograde transport system. Other components of the translocon such as Sec63p or the lumenal chaperone BiP may also be involved in export to the cytosol. Novel ER membrane proteins such as Der1p, Der3p/Hrd1p, or Hrd3p might reprogram the translocon for retrograde transport. As ubiquitination is a prerequisite for degradation by the proteasome, exported proteins are ubiquitinated. Representatives of ER membrane-bound ubiquitin-conjugating enzymes, Ubc6p and Cue1p/Ubc7p, have been identified in yeast. Retrograde transport and ubiquitination seem to be coupled processes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0892-6638
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1227-33
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Endoplasmic reticulum degradation: reverse protein flow of no return.
pubmed:affiliation
Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't