Linked Life Data

2553741

Source:http://linkedlifedata.com/resource/pubmed/id/2553741

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1989-12-5
pubmed:abstractText
The influenza A virus M2 polypeptide is a small integral membrane protein that does not contain a cleaved signal sequence, but is unusual in that it assumes the membrane orientation of a class I integral membrane protein with an NH2-terminal ectodomain and a COOH-terminal cytoplasmic tail. To determine the domains of M2 involved in specifying membrane orientation, hybrid genes were constructed and expressed in which regions of the M2 protein were linked to portions of the paramyxovirus HN and SH proteins, two class II integral membrane proteins that adopt the opposite orientation in membranes from M2. A hybrid protein (MgMH) consisting of the M2 NH2-terminal and membrane-spanning domains linked precisely to the HN COOH-terminal ectodomain was found in cells in two forms: integrated into membranes in the M2 topology or completely translocated across the endoplasmic reticulum membrane and ultimately secreted from the cell. The finding of a soluble form suggested that in this hybrid protein the anchor function of the M2 signal/anchor domain can be overridden. A second hybrid which contained the M2 NH2 terminus linked to the HN signal anchor and ectodomain (MgHH) was found in both the M2 and the HN orientation, suggesting that the M2 NH2 terminus was capable of reversing the topology of a class II membrane protein. The exchange of the M2 signal/anchor domain with that of SH resulted in a hybrid protein which assumed only the M2 topology. Thus, all these data suggest that the NH2-terminal 24 residues to M2 are important for directing the unusual membrane topology of the M2 protein. These data are discussed in relationship to the loop model for insertion of proteins into membranes and the role of charged residues as a factor in determining orientation.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-197698, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-2455818, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-2536819, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-2784443, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-2836432, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-2836617, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-2845415, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-2993864, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3023882, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3025652, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3026647, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3030381, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3047140, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3095828, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3198683, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3290220, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3418787, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3530500, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3678203, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3753585, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3791411, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3840537, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3865176, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3882238, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-3886166, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-4020965, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-4048938, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-6090955, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-6184879, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-6225933, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-6253998, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-6300656, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-6326121, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-6327078, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-6361451, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-6587354, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-6929499, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-7035466, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-726267, http://linkedlifedata.com/resource/pubmed/commentcorrection/2553741-982840
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:volume
109
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2023-32
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Transposition of domains between the M2 and HN viral membrane proteins results in polypeptides which can adopt more than one membrane orientation.
pubmed:affiliation
Department of Biochemistry, Northwestern University, Evanston, Illinois 60208-3500.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't