Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M411220200 on November 30, 2004

J. Biol. Chem., Vol. 280, Issue 7, 5972-5982, February 18, 2005
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
280/7/5972    most recent
M411220200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Collins, M. O.
Right arrow Articles by Grant, S. G. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Collins, M. O.
Right arrow Articles by Grant, S. G. N.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Proteomic Analysis of in Vivo Phosphorylated Synaptic Proteins*{boxs}

Mark O. Collins{ddagger}§, Lu Yu§, Marcelo P. Coba§, Holger Husi{ddagger}, Iain Campuzano¶, Walter P. Blackstock||, Jyoti S. Choudhary§, and Seth G. N. Grant{ddagger}§**

From the {ddagger}Division of Neuroscience, University of Edinburgh, Edinburgh EH8 9JZ, United Kingdom, the §Wellcome Trust Sanger Institute, Hinxton CB10 1SA, United Kingdom, Waters Corp., Manchester M22 5PP, United Kingdom, and the ||Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, United Kingdom

In the nervous system, protein phosphorylation is an essential feature of synaptic function. Although protein phosphorylation is known to be important for many synaptic processes and in disease, little is known about global phosphorylation of synaptic proteins. Heterogeneity and low abundance make protein phosphorylation analysis difficult, particularly for mammalian tissue samples. Using a new approach, combining both protein and peptide immobilized metal affinity chromatography and mass spectrometry data acquisition strategies, we have produced the first large scale map of the mouse synapse phosphoproteome. We report over 650 phosphorylation events corresponding to 331 sites (289 have been unambiguously assigned), 92% of which are novel. These represent 79 proteins, half of which are novel phosphoproteins, and include several highly phosphorylated proteins such as MAP1B (33 sites) and Bassoon (30 sites). An additional 149 candidate phosphoproteins were identified by profiling the composition of the protein immobilized metal affinity chromatography enrichment. All major synaptic protein classes were observed, including components of important pre- and postsynaptic complexes as well as low abundance signaling proteins. Bioinformatic and in vitro phosphorylation assays of peptide arrays suggest that a small number of kinases phosphorylate many proteins and that each substrate is phosphorylated by many kinases. These data substantially increase existing knowledge of synapse protein phosphorylation and support a model where the synapse phosphoproteome is functionally organized into a highly interconnected signaling network.

Received for publication, September 30, 2004 , and in revised form, November 16, 2004.

* This work was spported by the Wellcome Trust (to H. H., J. S. C., L. Y., M. O. C., M. P. C., and S. G. N. G.) and the Biotechnology and Biological Sciences Research Council (to M. O. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{boxs} The on-line version of this article (available at http://www.jbc.org) contains an additional figure and four tables.

** To whom correspondence should be addressed: Wellcome Trust Sanger Institute, Hinxton, Cambridgeshire CB10 1SA, United Kingdom. Tel.: 44-1223-494-908; Fax: 44-1233-494-919; E-mail: sg3{at}sanger.ac.uk.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Cell Sci.Home page
T. M. E. Scales, S. Lin, M. Kraus, R. G. Goold, and P. R. Gordon-Weeks
Nonprimed and DYRK1A-primed GSK3{beta}-phosphorylation sites on MAP1B regulate microtubule dynamics in growing axons
J. Cell Sci., July 15, 2009; 122(14): 2424 - 2435.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
R. J. Chalkley, A. Thalhammer, R. Schoepfer, and A. L. Burlingame
Identification of protein O-GlcNAcylation sites using electron transfer dissociation mass spectrometry on native peptides
PNAS, June 2, 2009; 106(22): 8894 - 8899.
[Abstract] [Full Text] [PDF]

Home page
 Sci SignalHome page
M. P. Coba, A. J. Pocklington, M. O. Collins, M. V. Kopanitsa, R. T. Uren, S. Swamy, M. D. R. Croning, J. S. Choudhary, and S. G. N. Grant
Neurotransmitters Drive Combinatorial Multistate Postsynaptic Density Networks
Sci. Signal., April 28, 2009; 2(68): ra19 - ra19.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
D. Edbauer, D. Cheng, M. N. Batterton, C.-F. Wang, D. M. Duong, M. B. Yaffe, J. Peng, and M. Sheng
Identification and Characterization of Neuronal Mitogen-activated Protein Kinase Substrates Using a Specific Phosphomotif Antibody
Mol. Cell. Proteomics, April 1, 2009; 8(4): 681 - 695.
[Abstract] [Full Text] [PDF]

Home page
 GENES CELLSHome page
K. Sugawara, T. Shibasaki, A. Mizoguchi, T. Saito, and S. Seino
Rab11 and its effector Rip11 participate in regulation of insulin granule exocytosis.
Genes Cells, April 1, 2009; 14(4): 445 - 456.
[Abstract] [Full Text] [PDF]

Home page
 EndocrinologyHome page
M. D. Seferovic, R. Ali, H. Kamei, S. Liu, J. M. Khosravi, S. Nazarian, V. K. M. Han, C. Duan, and M. B. Gupta
Hypoxia and Leucine Deprivation Induce Human Insulin-Like Growth Factor Binding Protein-1 Hyperphosphorylation and Increase Its Biological Activity
Endocrinology, January 1, 2009; 150(1): 220 - 231.
[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
 Mol. Cell. ProteomicsHome page
M. O. Collins, L. Yu, I. Campuzano, S. G. N. Grant, and J. S. Choudhary
Phosphoproteomic Analysis of the Mouse Brain Cytosol Reveals a Predominance of Protein Phosphorylation in Regions of Intrinsic Sequence Disorder
Mol. Cell. Proteomics, July 1, 2008; 7(7): 1331 - 1348.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. H. Reynolds, C. J. Garwood, S. Wray, C. Price, S. Kellie, T. Perera, M. Zvelebil, A. Yang, P. W. Sheppard, I. M. Varndell, et al.
Phosphorylation Regulates Tau Interactions with Src Homology 3 Domains of Phosphatidylinositol 3-Kinase, Phospholipase C{gamma}1, Grb2, and Src Family Kinases
J. Biol. Chem., June 27, 2008; 283(26): 18177 - 18186.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
J. C. Trinidad, A. Thalhammer, C. G. Specht, A. J. Lynn, P. R. Baker, R. Schoepfer, and A. L. Burlingame
Quantitative Analysis of Synaptic Phosphorylation and Protein Expression
Mol. Cell. Proteomics, April 1, 2008; 7(4): 684 - 696.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
J. Y. Delgado, M. Coba, C. N. G. Anderson, K. R. Thompson, E. E. Gray, C. L. Heusner, K. C. Martin, S. G. N. Grant, and T. J. O'Dell
NMDA Receptor Activation Dephosphorylates AMPA Receptor Glutamate Receptor 1 Subunits at Threonine 840
J. Neurosci., November 28, 2007; 27(48): 13210 - 13221.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. Hlavanda, E. Klement, E. Kokai, J. Kovacs, O. Vincze, N. Tokesi, F. Orosz, K. F. Medzihradszky, V. Dombradi, and J. Ovadi
Phosphorylation Blocks the Activity of Tubulin Polymerization-promoting Protein (TPPP): IDENTIFICATION OF SITES TARGETED BY DIFFERENT KINASES
J. Biol. Chem., October 5, 2007; 282(40): 29531 - 29539.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
A. Dosemeci, A. J. Makusky, E. Jankowska-Stephens, X. Yang, D. J. Slotta, and S. P. Markey
Composition of the Synaptic PSD-95 Complex
Mol. Cell. Proteomics, October 1, 2007; 6(10): 1749 - 1760.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
S. Y. Imanishi, V. Kochin, S. E. Ferraris, A. de Thonel, H.-M. Pallari, G. L. Corthals, and J. E. Eriksson
Reference-facilitated Phosphoproteomics: FAST AND RELIABLE PHOSPHOPEPTIDE VALIDATION BY {micro}LC-ESI-Q-TOF MS/MS
Mol. Cell. Proteomics, August 1, 2007; 6(8): 1380 - 1391.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
J. Villen, S. A. Beausoleil, S. A. Gerber, and S. P. Gygi
Large-scale phosphorylation analysis of mouse liver
PNAS, January 30, 2007; 104(5): 1488 - 1493.
[Abstract] [Full Text] [PDF]

Home page
 Integr. Comp. Biol.Home page
S. G. Lee and D. L. Mykles
Proteomics and signal transduction in the crustacean molting gland
Integr. Comp. Biol., December 1, 2006; 46(6): 965 - 977.
[Abstract] [Full Text] [PDF]

Home page
 J. Pharmacol. Exp. Ther.Home page
N. S. Abul-Husn and L. A. Devi
Neuroproteomics of the Synapse and Drug Addiction
J. Pharmacol. Exp. Ther., August 1, 2006; 318(2): 461 - 468.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
S.-H. Liu, H.-H. Cheng, S.-Y. Huang, P.-C. Yiu, and Y.-C. Chang
Studying the Protein Organization of the Postsynaptic Density by a Novel Solid Phase- and Chemical Cross-linking-based Technology
Mol. Cell. Proteomics, June 1, 2006; 5(6): 1019 - 1032.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
K. Vosseller, J. C. Trinidad, R. J. Chalkley, C. G. Specht, A. Thalhammer, A. J. Lynn, J. O. Snedecor, S. Guan, K. F. Medzihradszky, D. A. Maltby, et al.
O-Linked N-Acetylglucosamine Proteomics of Postsynaptic Density Preparations Using Lectin Weak Affinity Chromatography and Mass Spectrometry
Mol. Cell. Proteomics, May 1, 2006; 5(5): 923 - 934.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
H. Steen, J. A. Jebanathirajah, J. Rush, N. Morrice, and M. W. Kirschner
Phosphorylation Analysis by Mass Spectrometry: Myths, Facts, and the Consequences for Qualitative and Quantitative Measurements
Mol. Cell. Proteomics, January 1, 2006; 5(1): 172 - 181.
[Abstract] [Full Text] [PDF]

Home page
 Sci SignalHome page
M. O. Collins, L. Yu, H. Husi, W. P. Blackstock, J. S. Choudhary, and S. G. N. Grant
Robust Enrichment of Phosphorylated Species in Complex Mixtures by Sequential Protein and Peptide Metal-Affinity Chromatography and Analysis by Tandem Mass Spectrometry
Sci. Signal., August 23, 2005; 2005(298): pl6 - pl6.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. ProteomicsHome page
A. Gruhler, J. V. Olsen, S. Mohammed, P. Mortensen, N. J. Faergeman, M. Mann, and O. N. Jensen
Quantitative Phosphoproteomics Applied to the Yeast Pheromone Signaling Pathway
Mol. Cell. Proteomics, March 1, 2005; 4(3): 310 - 327.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement