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Stress-activated Protein Kinase-3 Interacts with the PDZ Domain of α1-Syntrophin
Open accessAbstract
Mechanisms for selective targeting to unique subcellular sites play an important role in determining the substrate specificities of protein kinases. Here we show that stress-activated protein kinase-3 (SAPK3, also called ERK6 and p38gamma), a member of the mitogen-activated protein kinase family that is abundantly expressed in skeletal muscle, binds through its carboxyl-terminal sequence -KETXL to the PDZ domain of alpha1-syntrophin. SAPK3 phosphorylates alpha1-syntrophin at serine residues 193 and 201 in vitro and phosphorylation is dependent on binding to the PDZ domain of alpha1-syntrophin. In skeletal muscle SAPK3 and alpha1-syntrophin co-localize at the neuromuscular junction, and both proteins can be co-immunoprecipitated from transfected COS cell lysates. Phosphorylation of a PDZ domain-containing protein by an associated protein kinase is a novel mechanism for determining both the localization and the substrate specificity of a protein kinase.
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Cites
Hibi, M., Lin, A., Smeal, T., Minden, A., & Karin, M. (1993) · Genes & Development · doi:10.1101/gad.7.11.2135 · Cited by 1,886
Butz, S., Okamoto, M., & Südhof, T. C. (1998) · Cell · doi:10.1016/s0092-8674(00)81736-5 · Cited by 548
Cited by
Allen, D. G., Whitehead, N. P., & Froehner, S. C. (2016) · Physiological Reviews · doi:10.1152/physrev.00007.2015 · Cited by 426
BIRB796 Inhibits All p38 MAPK Isoforms in Vitro and in Vivo
Kuma, Y., Sabio, G., Bain, J., Shpiro, N., Márquez, R., & Cuenda, A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414221200 · Cited by 304
Self-citationP38-γ–dependent gene silencing restricts entry into the myogenic differentiation program
Gillespie, M. A., Le Grand, F., Scimè, A., Kuang, S., von Maltzahn, J., Seale, V., Cuenda, A., Ranish, J. A., & Rudnicki, M. A. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200907037 · Cited by 131
γ-Syntrophin scaffolding is spatially and functionally distinct from that of the α/β syntrophins
Alessi, A., Bragg, A. D., Percival, J. M., Yoo, J., Albrecht, D. E., Froehner, S. C., & Adams, M. E. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.06.019 · Cited by 60
Metadata
- Authors
- Hasegawa, M., Cuenda, A., Spillantini, M. G., Thomas, G. M., Buée-Scherrer, V., Cohen, P., & Goedert, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-04
- Volume
- 274
- Issue
- 18
- Pages
- 12626-12631
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2087430420
- Cited by
- 158
- References
- 2
- FWCI
- 4.46
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- The paper
- Hasegawa, M., Cuenda, A., Spillantini, M. G., Thomas, G. M., Buée-Scherrer, V., Cohen, P., & Goedert, M. (1999). Stress-activated Protein Kinase-3 Interacts with the PDZ Domain of α1-Syntrophin. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.18.12626
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