Skip Navigation


Human Molecular Genetics Advance Access originally published online on September 8, 2005
Human Molecular Genetics 2005 14(Review Issue 2):R225-R234; doi:10.1093/hmg/ddi330
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Supplementary Material
Right arrow All Versions of this Article:
14/suppl_2/R225    most recent
ddi330v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Grant, S. G.N.
Right arrow Articles by Armstrong, J. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Grant, S. G.N.
Right arrow Articles by Armstrong, J. D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2005. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Synapse proteomics of multiprotein complexes: en route from genes to nervous system diseases

Seth G.N. Grant1,*, Michael C. Marshall1, Keri-Lee Page1, Mark A. Cumiskey1,2 and J. Douglas Armstrong2

1Wellcome Trust Sanger Institute, Hinxton, Cambridgeshire CB10 1SA, UK and 2School of Informatics, Edinburgh University, UK

* To whom correspondence should be addressed. Tel: +44 1223494908; Email: sg3{at}sanger.ac.uk

Received July 5, 2005; Accepted August 25, 2005

Proteomic experiments have produced a draft profile of the overall molecular composition of the mammalian neuronal synapse. It appears that synapses have over 1000 protein components and the mapping of their interactions, organization and functions will lead to a global view of the role of synapses in physiology and disease. A major functional subcomponent of the synaptic machinery is a multiprotein complex of glutamate receptors and adhesion proteins with associated adaptor and signalling enzymes totally 185 proteins known as the N-methyl-D-aspartate receptor complex/MAGUK associated signalling complex (NRC/MASC). Here, we review the proteomic studies and functions of NRC/MASC and specifically report on the role of its component genes in human diseases. Using a systematic literature search protocol, we identified reports of mutations or polymorphisms in 47 genes associated with 183 disorders, of which 54 were nervous system disorders. A similar number of genes are important in mouse synaptic plasticity and behaviour, where the NRC/MASC acts as a signalling complex with multiple functions provided by its individual protein components and their interactions. The individual gene mutations suggest not only an important role for the NRC/MASC in human diseases but that these diseases may be functionally connected by their common link to the NRC/MASC. The NRC/MASC is a rich source of genetic variation and provides a platform for understanding relationships of disease phenotype amenable to systematic studies such as the Genes to Cognition research consortium (www.genes2cognition.org) that links human and mouse genetics with proteomic studies.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
M. D. R. Croning, M. C. Marshall, P. McLaren, J. D. Armstrong, and S. G. N. Grant
G2Cdb: the Genes to Cognition database
Nucleic Acids Res., January 1, 2009; 37(suppl_1): D846 - D851.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
H. J. Carlisle, A. E. Fink, S. G. N. Grant, and T. J. O'Dell
Opposing effects of PSD-93 and PSD-95 on long-term potentiation and spike timing-dependent plasticity
J. Physiol., December 15, 2008; 586(24): 5885 - 5900.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. P. Coba, L. M. Valor, M. V. Kopanitsa, N. O. Afinowi, and S. G. N. Grant
Kinase Networks Integrate Profiles of N-Methyl-D-aspartate Receptor-mediated Gene Expression in Hippocampus
J. Biol. Chem., December 5, 2008; 283(49): 34101 - 34107.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
L. S. Wijetunge, S. M. Till, T. H. Gillingwater, C. A. Ingham, and P. C. Kind
mGluR5 Regulates Glutamate-Dependent Development of the Mouse Somatosensory Cortex
J. Neurosci., December 3, 2008; 28(49): 13028 - 13037.
[Abstract] [Full Text] [PDF]

Home page
 J PsychopharmacolHome page
S. L. Eastwood, L. Lyon, L. George, A. Andrieux, D. Job, and P. J. Harrison
Altered expression of synaptic protein mRNAs in STOP (MAP6) mutant mice
J Psychopharmacol, August 1, 2007; 21(6): 635 - 644.
[Abstract] [PDF]

Home page
 J. Neurosci.Home page
P. C. Cuthbert, L. E. Stanford, M. P. Coba, J. A. Ainge, A. E. Fink, P. Opazo, J. Y. Delgado, N. H. Komiyama, T. J. O'Dell, and S. G. N. Grant
Synapse-Associated Protein 102/dlgh3 Couples the NMDA Receptor to Specific Plasticity Pathways and Learning Strategies
J. Neurosci., March 7, 2007; 27(10): 2673 - 2682.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.