Linked Life Data

7721788

Source:http://linkedlifedata.com/resource/pubmed/id/7721788

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
1995-5-19
pubmed:abstractText
The mouse hepatitis virus M protein is a triple spanning membrane glycoprotein that, when expressed independently, localizes to trans-Golgi as well as to the trans-Golgi network (TGN). Passage of this protein from the endoplasmic reticulum through the intermediate compartment to the late Golgi and TGN can be conveniently followed by analyzing its O-linked sugars. Using pulse-chase analyses we studied the oligomerization of the M protein in sucrose gradients. The Golgi and TGN forms migrated as large heterogeneous complexes, whereas the endoplasmic reticulum and intermediate compartment forms of the protein appeared to migrate as monomer. Moreover, a mutant of the M protein lacking the 22 COOH-terminal amino acids, that is transported to the plasma membrane, gave rise to similar complexes, albeit smaller in size, that persisted at the plasma membrane. We propose that the trans-Golgi/TGN retention of the MHV-M protein is governed by two mechanisms: oligomerization possibly mediated by the transmembrane domains and binding of its cytoplasmic tail to cellular factors in trans Golgi/TGN.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8815-21
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Oligomerization of a trans-Golgi/trans-Golgi network retained protein occurs in the Golgi complex and may be part of its retention.
pubmed:affiliation
Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, Utrecht University, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't