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Sci. Signal., 2 September 2008
Vol. 1, Issue 35, p. ra2
[DOI: 10.1126/scisignal.1159433]
RESEARCH ARTICLES
Editor's Summary
An Atlas of Phosphorylation
NetPhorest is a community resource that uses phylogenetic trees to organize data from both in vivo and in vitro experiments to derive sequence specificities for 179 kinases and 104 domains (SH2, PTB, BRCT, WW, and 14–3–3) that bind to phosphorylated sites. The resulting atlas of linear motifs revealed that oncogenic kinases tend to be less specific in the target sequences they phosphorylate than their non-oncogenic counterparts, that autophosphorylation sites tend to be more variable than other substrates of a given kinase, and that coupling interaction domains with kinase domains may allow phosphorylation site specificity to be low while still maintaining substrate specificity.
Citation: M. L. Miller, L. J. Jensen, F. Diella, C. Jørgensen, M. Tinti, L. Li, M. Hsiung, S. A. Parker, J. Bordeaux, T. Sicheritz-Ponten, M. Olhovsky, A. Pasculescu, J. Alexander, S. Knapp, N. Blom, P. Bork, S. Li, G. Cesareni, T. Pawson, B. E. Turk, M. B. Yaffe, S. Brunak, R. Linding, Linear Motif Atlas for Phosphorylation-Dependent Signaling. Sci. Signal.1, ra2 (2008).
Janine Mok, Philip M. Kim, Hugo Y. K. Lam, Stacy Piccirillo, Xiuqiong Zhou, Grace R. Jeschke, Douglas L. Sheridan, Sirlester A. Parker, Ved Desai, Miri Jwa, Elisabetta Cameroni, Hengyao Niu, Matthew Good, Attila Remenyi, Jia-Lin Nianhan Ma, Yi-Jun Sheu, Holly E. Sassi, Richelle Sopko, Clarence S. M. Chan, Claudio De Virgilio, Nancy M. Hollingsworth, Wendell A. Lim, David F. Stern, Bruce Stillman, Brenda J. Andrews, Mark B. Gerstein, Michael Snyder, and Benjamin E. Turk (16 February 2010) Sci. Signal.3 (109), ra12.
[DOI: 10.1126/scisignal.2000482] |Editor's Summary »|Abstract »|Full Text »|PDF »|Supplementary Materials »
RESEARCH ARTICLES
Chris Soon Heng Tan, Bernd Bodenmiller, Adrian Pasculescu, Marko Jovanovic, Michael O. Hengartner, Claus Jørgensen, Gary D. Bader, Ruedi Aebersold, Tony Pawson, and Rune Linding (28 July 2009) Sci. Signal.2 (81), ra39.
[DOI: 10.1126/scisignal.2000316] |Editor's Summary »|Abstract »|Full Text »|PDF »|Supplementary Materials »
PODCASTS
Ulrik B. Nielsen and Annalisa M. VanHook (30 June 2009) Sci. Signal.2 (77), pc12.
[DOI: 10.1126/scisignal.277pc12] |Abstract »|Full Text »|Podcast »
EDITORS' CHOICE
Wei Wong (7 April 2009) Sci. Signal.2 (65), ec126.
[DOI: 10.1126/scisignal.265ec126] |Abstract »
PODCASTS
Rune Linding and Annalisa M. VanHook (28 October 2008) Sci. Signal.1 (43), pc10.
[DOI: 10.1126/scisignal.143pc10] |Abstract »|Full Text »|Podcast »
EDITORS' CHOICE
Elizabeth M. Adler (3 July 2007) Sci. STKE2007 (393), tw231.
[DOI: 10.1126/stke.3932007tw231] |Abstract »
In Vivo Phosphoproteomics Analysis Reveals the Cardiac Targets of {beta}-Adrenergic Receptor Signaling.
A. Lundby, M. N. Andersen, A. B. Steffensen, H. Horn, C. D. Kelstrup, C. Francavilla, L. J. Jensen, N. Schmitt, M. B. Thomsen, and J. V. Olsen (2013)
Science Signaling
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Phosphotyrosine Signaling Proteins that Drive Oncogenesis Tend to be Highly Interconnected.
G. Koytiger, A. Kaushansky, A. Gordus, J. Rush, P. K. Sorger, and G. MacBeath (2013)
Mol. Cell. Proteomics
12, 1204-1213
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Genetics and Phosphoproteomics Reveal a Protein Phosphorylation Network in the Abscisic Acid Signaling Pathway in Arabidopsis thaliana.
T. Umezawa, N. Sugiyama, F. Takahashi, J. C. Anderson, Y. Ishihama, S. C. Peck, and K. Shinozaki (2013)
Science Signaling
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The Tumor Suppressor Mst1 Promotes Changes in the Cellular Redox State by Phosphorylation and Inactivation of Peroxiredoxin-1 Protein.
S. J. Rawat, C. L. Creasy, J. R. Peterson, and J. Chernoff (2013)
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Computational phosphorylation site prediction in plants using random forests and organism-specific instance weights.
Involvement of Lyn and the Atypical Kinase SgK269/PEAK1 in a Basal Breast Cancer Signaling Pathway.
D. R. Croucher, F. Hochgrafe, L. Zhang, L. Liu, R. J. Lyons, D. Rickwood, C. M. Tactacan, B. C. Browne, N. Ali, H. Chan, et al. (2013)
Cancer Res.
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Systems biology in physiology: the vasopressin signaling network in kidney.
SAPIN: A framework for the structural analysis of protein interaction networks.
J.-S. Yang, A. Campagna, J. Delgado, P. Vanhee, L. Serrano, and C. Kiel (2012)
Bioinformatics
28, 2998-2999
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Cyclic GMP-dependent Stimulation of Serotonin Transport Does Not Involve Direct Transporter Phosphorylation by cGMP-dependent Protein Kinase.
A. Wong, Y.-W. Zhang, G. R. Jeschke, B. E. Turk, and G. Rudnick (2012)
J. Biol. Chem.
287, 36051-36058
|Abstract »|Full Text »|PDF »
Identifying protein kinase target preferences using mass spectrometry.
J. Douglass, R. Gunaratne, D. Bradford, F. Saeed, J. D. Hoffert, P. J. Steinbach, M. A. Knepper, and T. Pisitkun (2012)
Am J Physiol Cell Physiol
303, C715-C727
|Abstract »|Full Text »|PDF »
Protein kinases display minimal interpositional dependence on substrate sequence: potential implications for the evolution of signalling networks.
B. A. Joughin, C. Liu, D. A. Lauffenburger, C. W. V. Hogue, and M. B. Yaffe (2012)
Phil Trans R Soc B
367, 2574-2583
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Modular evolution of phosphorylation-based signalling systems.
Charting the Landscape of Tandem BRCT Domain-Mediated Protein Interactions.
N. T. Woods, R. D. Mesquita, M. Sweet, M. A. Carvalho, X. Li, Y. Liu, H. Nguyen, C. E. Thomas, E. S. Iversen Jr., S. Marsillac, et al. (2012)
Science Signaling
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PepSite: prediction of peptide-binding sites from protein surfaces.
L. G. Trabuco, S. Lise, E. Petsalaki, and R. B. Russell (2012)
Nucleic Acids Res.
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The human phosphotyrosine signaling network: Evolution and hotspots of hijacking in cancer.
L. Li, C. Tibiche, C. Fu, T. Kaneko, M. F. Moran, M. R. Schiller, S. S.-C. Li, and E. Wang (2012)
Genome Res.
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MMFPh: a maximal motif finder for phosphoproteomics datasets.
T. Wang, A. N. Kettenbach, S. A. Gerber, and C. Bailey-Kellogg (2012)
Bioinformatics
28, 1562-1570
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C-terminal Acidic Cluster Is Involved in Ca2+-induced Regulation of Human Transient Receptor Potential Ankyrin 1 Channel.
L. Sura, V. Zima, L. Marsakova, A. Hynkova, I. Barvik, and V. Vlachova (2012)
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287, 18067-18077
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L. R. Barkley, K. Palle, M. Durando, T. A. Day, A. Gurkar, N. Kakusho, J. Li, H. Masai, and C. Vaziri (2012)
Mol. Biol. Cell
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Crk and Abi1: Binary Molecular Switches That Regulate Abl Tyrosine Kinase and Signaling to the Cytoskeleton.
S. Hossain, P. M. Dubielecka, A. F. Sikorski, R. B. Birge, and L. Kotula (2012)
Genes & Cancer
3, 402-413
|Abstract »|Full Text »|PDF »
MUSI: an integrated system for identifying multiple specificity from very large peptide or nucleic acid data sets.
T. Kim, M. S. Tyndel, H. Huang, S. S. Sidhu, G. D. Bader, D. Gfeller, and P. M. Kim (2012)
Nucleic Acids Res.
40, e47
|Abstract »|Full Text »|PDF »
Phosphosite Mapping of P-type Plasma Membrane H+-ATPase in Homologous and Heterologous Environments.
E. L. Rudashevskaya, J. Ye, O. N. Jensen, A. T. Fuglsang, and M. G. Palmgren (2012)
J. Biol. Chem.
287, 4904-4913
|Abstract »|Full Text »|PDF »
Dynamics of the G Protein-coupled Vasopressin V2 Receptor Signaling Network Revealed by Quantitative Phosphoproteomics.
J. D. Hoffert, T. Pisitkun, F. Saeed, J. H. Song, C.-L. Chou, and M. A. Knepper (2012)
Mol. Cell. Proteomics
11, M111.014613
|Abstract »|Full Text »|PDF »
PlateletWeb: a systems biologic analysis of signaling networks in human platelets.
D. Boyanova, S. Nilla, I. Birschmann, T. Dandekar, and M. Dittrich (2012)
Blood
119, e22-e34
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Large-scale phosphotyrosine proteomic profiling of rat renal collecting duct epithelium reveals predominance of proteins involved in cell polarity determination.
B. Zhao, M. A. Knepper, C.-L. Chou, and T. Pisitkun (2012)
Am J Physiol Cell Physiol
302, C27-C45
|Abstract »|Full Text »|PDF »
The SH2 Domain-Containing Proteins in 21 Species Establish the Provenance and Scope of Phosphotyrosine Signaling in Eukaryotes.
B. A. Liu, E. Shah, K. Jablonowski, A. Stergachis, B. Engelmann, and P. D. Nash (2011)
Science Signaling
4, ra83
|Abstract »|Full Text »|PDF »
Ajuba is required for Rac activation and maintenance of E-cadherin adhesion.
S. Nola, R. Daigaku, K. Smolarczyk, M. Carstens, B. Martin-Martin, G. Longmore, M. Bailly, and V. M. M. Braga (2011)
J. Cell Biol.
195, 855-871
|Abstract »|Full Text »|PDF »
Proteomic and Functional Genomic Landscape of Receptor Tyrosine Kinase and Ras to Extracellular Signal-Regulated Kinase Signaling.
A. A. Friedman, G. Tucker, R. Singh, D. Yan, A. Vinayagam, Y. Hu, R. Binari, P. Hong, X. Sun, M. Porto, et al. (2011)
Science Signaling
4, rs10
|Abstract »|Full Text »|PDF »
Sequence, Structure, and Network Evolution of Protein Phosphorylation.
Response to Comment on "Positive Selection of Tyrosine Loss in Metazoan Evolution".
C. S. H. Tan, E. M. Schoof, P. Creixell, A. Pasculescu, W. A. Lim, T. Pawson, G. D. Bader, and R. Linding (2011)
Science
332, 917
|Abstract »|Full Text »|PDF »
Identification of New Substrates of the Protein-tyrosine Phosphatase PTP1B by Bayesian Integration of Proteome Evidence.
E. Ferrari, M. Tinti, S. Costa, S. Corallino, A. P. Nardozza, A. Chatraryamontri, A. Ceol, G. Cesareni, and L. Castagnoli (2011)
J. Biol. Chem.
286, 4173-4185
|Abstract »|Full Text »|PDF »
The Plk1-dependent Phosphoproteome of the Early Mitotic Spindle.
A. Santamaria, B. Wang, S. Elowe, R. Malik, F. Zhang, M. Bauer, A. Schmidt, H. H. W. Sillje, R. Korner, and E. A. Nigg (2011)
Mol. Cell. Proteomics
10, M110.004457
|Abstract »|Full Text »|PDF »
Structural Bases of PAS Domain-regulated Kinase (PASK) Activation in the Absence of Activation Loop Phosphorylation.
C. K. Kikani, S. A. Antonysamy, J. B. Bonanno, R. Romero, F. F. Zhang, M. Russell, T. Gheyi, M. Iizuka, S. Emtage, J. M. Sauder, et al. (2010)
J. Biol. Chem.
285, 41034-41043
|Abstract »|Full Text »|PDF »
A Strategy for Interaction Site Prediction between Phospho-binding Modules and their Partners Identified from Proteomic Data.
W. Aucher, E. Becker, E. Ma, S. Miron, A. Martel, F. Ochsenbein, M.-C. Marsolier-Kergoat, and R. Guerois (2010)
Mol. Cell. Proteomics
9, 2745-2759
|Abstract »|Full Text »|PDF »
Musite, a Tool for Global Prediction of General and Kinase-specific Phosphorylation Sites.
J. Gao, J. J. Thelen, A. K. Dunker, and D. Xu (2010)
Mol. Cell. Proteomics
9, 2586-2600
|Abstract »|Full Text »|PDF »
Vasopressin increases phosphorylation of Ser84 and Ser486 in Slc14a2 collecting duct urea transporters.
S. Hwang, R. Gunaratne, M. M. Rinschen, M.-J. Yu, T. Pisitkun, J. D. Hoffert, R. A. Fenton, M. A. Knepper, and C.-L. Chou (2010)
Am J Physiol Renal Physiol
299, F559-F567
|Abstract »|Full Text »|PDF »
Collection and Motif-Based Prediction of Phosphorylation Sites in Human Viruses.
R. Gunaratne, D. W. W. Braucht, M. M. Rinschen, C.-L. Chou, J. D. Hoffert, T. Pisitkun, and M. A. Knepper (2010)
PNAS
107, 15653-15658
|Abstract »|Full Text »|PDF »
Dissecting the M Phase-specific Phosphorylation of Serine-Proline or Threonine-Proline Motifs.
C. F. Wu, R. Wang, Q. Liang, J. Liang, W. Li, S. Y. Jung, J. Qin, S. H. Lin, and J. Kuang (2010)
Mol. Biol. Cell
21, 1470-1481
|Abstract »|Full Text »|PDF »
Characterization of a Novel Interaction Between Vasodilator-Stimulated Phosphoprotein and Abelson Interactor 1 in Human Platelets: A Concerted Computational and Experimental Approach.
M. Dittrich, V. Strassberger, M. Fackler, P. Tas, U. Lewandrowski, A. Sickmann, U. Walter, T. Dandekar, and I. Birschmann (2010)
Arterioscler Thromb Vasc Biol
30, 843-850
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M. M. Rinschen, M.-J. Yu, G. Wang, E. S. Boja, J. D. Hoffert, T. Pisitkun, and M. A. Knepper (2010)
PNAS
107, 3882-3887
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Deciphering Protein Kinase Specificity Through Large-Scale Analysis of Yeast Phosphorylation Site Motifs.
J. Mok, P. M. Kim, H. Y. K. Lam, S. Piccirillo, X. Zhou, G. R. Jeschke, D. L. Sheridan, S. A. Parker, V. Desai, M. Jwa, et al. (2010)
Science Signaling
3, ra12
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Phosphoproteomic Profiling Reveals Vasopressin-Regulated Phosphorylation Sites in Collecting Duct.
A. D. Bansal, J. D. Hoffert, T. Pisitkun, S. Hwang, C.-L. Chou, E. S. Boja, G. Wang, and M. A. Knepper (2010)
J. Am. Soc. Nephrol.
21, 303-315
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Quantitative Phosphoproteomics Reveals Widespread Full Phosphorylation Site Occupancy During Mitosis.
J. V. Olsen, M. Vermeulen, A. Santamaria, C. Kumar, M. L. Miller, L. J. Jensen, F. Gnad, J. Cox, T. S. Jensen, E. A. Nigg, et al. (2010)
Science Signaling
3, ra3
|Abstract »|Full Text »|PDF »
Understanding protein phosphorylation on a systems level.
J. Lin, Z. Xie, H. Zhu, and J. Qian (2010)
Briefings in Functional Genomics
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ELM: the status of the 2010 eukaryotic linear motif resource.
C. M. Gould, F. Diella, A. Via, P. Puntervoll, C. Gemund, S. Chabanis-Davidson, S. Michael, A. Sayadi, J. C. Bryne, C. Chica, et al. (2010)
Nucleic Acids Res.
38, D167-D180
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Cell-Specific Information Processing in Segregating Populations of Eph Receptor Ephrin-Expressing Cells.
C. Jorgensen, A. Sherman, G. I. Chen, A. Pasculescu, A. Poliakov, M. Hsiung, B. Larsen, D. G. Wilkinson, R. Linding, and T. Pawson (2009)
Science
326, 1502-1509
|Abstract »|Full Text »|PDF »
Positive Selection of Tyrosine Loss in Metazoan Evolution.
C. S. H. Tan, A. Pasculescu, W. A. Lim, T. Pawson, G. D. Bader, and R. Linding (2009)
Science
325, 1686-1688
|Abstract »|Full Text »|PDF »
Comparative Analysis Reveals Conserved Protein Phosphorylation Networks Implicated in Multiple Diseases.
C. S. H. Tan, B. Bodenmiller, A. Pasculescu, M. Jovanovic, M. O. Hengartner, C. Jorgensen, G. D. Bader, R. Aebersold, T. Pawson, and R. Linding (2009)
Science Signaling
2, ra39
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Predicting Protein Post-translational Modifications Using Meta-analysis of Proteome Scale Data Sets.
D. Schwartz, M. F. Chou, and G. M. Church (2009)
Mol. Cell. Proteomics
8, 365-379
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Science Signaling Podcast: 28 October 2008.
R. Linding and A. M. VanHook (2008)
Science Signaling
1, pc10
|Abstract »|Full Text »