The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Phosphoprotein Analysis Using Antibodies Broadly Reactive against Phosphorylated Motifs
Open accessAbstract
The substrates of most protein kinases remain unknown because of the difficulty tracing signaling pathways and identifying sites of protein phosphorylation. Here we describe a method useful in detecting subclasses of protein kinase substrates. Although the method is broadly applicable to any protein kinase for which a substrate consensus motif has been identified, we illustrate here the use of antibodies broadly reactive against phosphorylated Ser/Thr-motifs typical of AGC kinase substrates. Phosphopeptide libraries with fixed residues corresponding to consensus motifs RXRXXT*/S* (Akt motif) and S*XR (protein kinase C motif) were used as antigens to generate antibodies that recognize many different phosphoproteins containing the fixed motif. Because most AGC kinase members are phosphorylated and activated by phosphoinositide-dependent protein kinase-1 (PDK1), we used PDK1-/- ES cells to profile potential AGC kinase substrates downstream of PDK1. To identify phosphoproteins detected using the Akt substrate antibody, we characterized the antibody binding specificity to generate a specificity matrix useful in predicting antibody reactivity. Using this approach we predicted and then identified a 30-kDa phosphoprotein detected by both Akt and protein kinase C substrate antibodies as S6 ribosomal protein. Phosphospecific motif antibodies offer a new approach to protein kinase substrate identification that combines immunoreactivity data with protein data base searches based upon antibody specificity.
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Cites
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
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Self-citationBlume-Jensen, P., & Hunter, T. (2001) · Nature · doi:10.1038/35077225 · Cited by 3,738
Phosphorylation and Activation of p70 s6k by PDK1
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Cited by
AKT/PKB signaling: navigating downstream
Manning, B. D., & Cantley, L. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.009 · Cited by 6,115
AMPK Phosphorylation of Raptor Mediates a Metabolic Checkpoint
Gwinn, D. M., Shackelford, D. B., Egan, D. F., Mihaylova, M. M., Mery, A., Vasquez, D. S., Turk, B. E., & Shaw, R. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.003 · Cited by 3,849
Proteomics by Mass Spectrometry: Approaches, Advances, and Applications
Yates, J. R., Ruse, C. I., & Nakorchevsky, A. (2009) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-061008-124934 · Cited by 1,078
Basu, S., Totty, N. F., Irwin, M. S., Sudol, M., & Downward, J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00776-1 · Cited by 843
S6K1- and ßTRCP-Mediated Degradation of PDCD4 Promotes Protein Translation and Cell Growth
Dorrello, N. V., Peschiaroli, A., Guardavaccaro, D., Colburn, N. H., Sherman, N. E., & Pagano, M. (2006) · Science · doi:10.1126/science.1130276 · Cited by 731
Schaffer, B. E., Levin, R. S., Hertz, N. T., Maures, T. J., Schoof, M. L., Hollstein, P. E., Benayoun, B. A., Banko, M. R., Shaw, R. J., Shokat, K. M., et al. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.09.009 · Cited by 184
Multiple Post-translational Modifications Affect Heterologous Protein Synthesis
Tokmakov, A. A., Kurotani, A., Takagi, T., Toyama, M., Shirouzu, M., Fukami, Y., & Yokoyama, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.366351 · Cited by 88
“Early estimates suggested that the majority of human proteins may be phosphorylated at multiple sites (in total 100000 sites) (62).”
BackgroundProteins and Proteoforms: New Separation Challenges
Regnier, F. E., & Kim, J. (2018) · Analytical Chemistry · doi:10.1021/acs.analchem.7b05007 · Cited by 36
Malik, A. U., Karapetsas, A., Nirujogi, R. S., Chatterjee, D., Phung, T. K., Wightman, M., Gourlay, R., Morrice, N., Mathea, S., Knapp, S., et al. (2022) · Biochemical Journal · doi:10.1042/bcj20220308 · Cited by 13
Self-citation
Metadata
- Authors
- Zhang, H., Zha, X., Tan, Y., Hornbeck, P. V., Mastrangelo, A. J., Alessi, D. R., Polakiewicz, R. D., & Comb, M. J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-10
- Volume
- 277
- Issue
- 42
- Pages
- 39379-39387
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1964211866
- Cited by
- 270
- References
- 4
- FWCI
- 7.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
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