Linked Life Data

11443120

Source:http://linkedlifedata.com/resource/pubmed/id/11443120

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
2001-10-1
pubmed:abstractText
Acetylcholinesterase (AChE) exists as AChE(H) and AChE(T) subunits, which differ by their C-terminal H or T peptides, generating glycophosphatidylinositol-anchored dimers and various oligomers, respectively. We introduced mutations in the four-helix bundle interface of glycophosphatidylinositol-anchored dimers, and analyzed their effect on the production and oligomerization of AChE(H), of AChE(T), and of truncated subunits, AChE(C) (without H or T peptide). Dimerization was reduced for all types of subunits, showing that they interact through the same contact zone; the formation of amphiphilic tetramers (Torpedo AChE(T)) and 13.5 S oligomers (rat AChE(T)) was also suppressed. Oligomerization appeared totally blocked by introduction of an N-linked glycan on the surface of helix alpha(7,8). Other point mutations did not affect the synthesis or the catalytic properties of AChE but reduced or blocked the secretion of AChE(T) subunits. Secretion of AChE(T) was partially restored by co-expression with Q(N), a secretable protein containing a proline-rich attachment domain (PRAD); Q(N) organized PRAD-linked tetramers, except for the N-glycosylated mutants. Thus, the simultaneous presence of an abnormal four-helix bundle zone and an exposed T peptide targeted the enzyme toward degradation, indicating a cross-talk between the catalytic and tetramerization domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
37379-89
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Acetylcholinesterase H and T dimers are associated through the same contact. Mutations at this interface interfere with the C-terminal T peptide, inducing degradation rather than secretion.
pubmed:affiliation
Laboratoire de Neurobiologie Cellulaire et Moléculaire, CNRS UMR 8544, Ecole Normale Supérieure, 46 rue d'Ulm, 75005 Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't