Linked Life Data

3359486

Source:http://linkedlifedata.com/resource/pubmed/id/3359486

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-6-3
pubmed:abstractText
Results from several systems indicate that correct protein folding and subunit assembly correlate with the transport of membrane and secretory proteins from the endoplasmic reticulum (ER) to the Golgi complex. Because the site of oligomer assembly and its precise relationship to intracellular transport remain unclear, we have studied in detail the folding and trimerization of the influenza virus hemagglutinin (HA0) relative to its transport from ER to Golgi. Trimerization and transport were analyzed using several different methods, including transport inhibitors, temperature blocks, semi-intact cells, in vitro protein translocation, and immunocytochemistry. Taken together, the results clearly demonstrate that trimerization occurs at a point prior to exit from the ER. Before assembly, HA0 monomers were extensively folded and possessed intramolecular disulfide bonds, but monomers were not transported to the cis Golgi compartment. Thus, hemagglutinin progresses through at least two intermediate states before transport to the Golgi: highly folded monomers and trimers that have not yet left the ER.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
53
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
197-209
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Folding, trimerization, and transport are sequential events in the biogenesis of influenza virus hemagglutinin.
pubmed:affiliation
Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't