Document Detail


Interaction with telencephalin and the amyloid precursor protein predicts a ring structure for presenilins.
MedLine Citation:
PMID:  11719200     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The carboxyl terminus of presenilin 1 and 2 (PS1 and PS2) binds to the neuron-specific cell adhesion molecule telencephalin (TLN) in the brain. PS1 deficiency results in the abnormal accumulation of TLN in a yet unidentified intracellular compartment. The first transmembrane domain and carboxyl terminus of PS1 form a binding pocket with the transmembrane domain of TLN. Remarkably, APP binds to the same regions via part of its transmembrane domain encompassing the critical residues mutated in familial Alzheimer's disease. Our data surprisingly indicate a spatial dissociation between the binding site and the proposed catalytic site near the critical aspartates in PSs. They provide important experimental evidence to support a ring structure model for PS.
Authors:
W G Annaert; C Esselens; V Baert; C Boeve; G Snellings; P Cupers; K Craessaerts; B De Strooper
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Neuron     Volume:  32     ISSN:  0896-6273     ISO Abbreviation:  Neuron     Publication Date:  2001 Nov 
Date Detail:
Created Date:  2001-11-23     Completed Date:  2002-01-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8809320     Medline TA:  Neuron     Country:  United States    
Other Details:
Languages:  eng     Pagination:  579-89     Citation Subset:  IM    
Affiliation:
Laboratory for Neuronal Cell Biology, Department of Human Genetics, Flanders Interuniversity Institute for Biotechnology, KUL-Gasthuisberg, B-3000 Leuven, Belgium. ad@med.kuleuven.ac.be
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MeSH Terms
Descriptor/Qualifier:
Amyloid beta-Protein Precursor / chemistry,  metabolism*
Animals
Binding Sites
Cell Differentiation
Gene Expression
Hippocampus / cytology
Membrane Glycoproteins / chemistry,  metabolism*
Membrane Proteins / chemistry*,  genetics,  metabolism
Mice
Mice, Knockout
Nerve Tissue Proteins / chemistry,  metabolism*
Neurons / cytology,  metabolism
Presenilin-1
Presenilin-2
Protein Structure, Tertiary
Two-Hybrid System Techniques
Chemical
Reg. No./Substance:
0/Amyloid beta-Protein Precursor; 0/Icam5 protein, mouse; 0/Membrane Glycoproteins; 0/Membrane Proteins; 0/Nerve Tissue Proteins; 0/Presenilin-1; 0/Presenilin-2

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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