Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase

Mitogen-Activated Protein Kinases: Specific Messages from Ubiquitous Messengers

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A conserved docking motif in MAP kinases common to substrates, activators and regulators

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Akt Enhances Mdm2-mediated Ubiquitination and Degradation of p53

Ogawara, Y., Kishishita, S., Obata, T., Isazawa, Y., Suzuki, T., Tanaka, K., Masuyama, N., & Gotoh, Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109745200 · Cited by 617

Mitogenic Activation, Phosphorylation, and Nuclear Translocation of Protein Kinase Bβ

Meier, R., Alessi, D. R., Cron, P., Andjelković, M., & Hemmings, B. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.48.30491 · Cited by 378

Identification of a docking groove on ERK and p38 MAP kinases that regulates the specificity of docking interactions

Tanoue, T., Maeda, R., Adachi, M., & Nishida, E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.3.466 · Cited by 285

Docking Motif Interactions in MAP Kinases Revealed by Hydrogen Exchange Mass Spectrometry

Lee, T., Hoofnagle, A. N., Kabuyama, Y., Stroud, J., Min, X., Goldsmith, E. J., Chen, L., Resing, K. A., & Ahn, N. G. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00161-3 · Cited by 282

ERK2 is required for efficient terminal differentiation of skeletal myoblasts

Li, J., & Johnson, S. E. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.051 · Cited by 137

Docking interactions in the mitogen-activated protein kinase cascades

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Nlk is a murine protein kinase related to Erk/MAP kinases and localized in the nucleus

Brott, B. K., Pinsky, B. A., & Erikson, R. L. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.3.963 · Cited by 130

Spatially Separate Docking Sites on ERK2 Regulate Distinct Signaling Events In Vivo

Dimitri, C. A., Dowdle, W., MacKeigan, J. P., Blenis, J., & Murphy, L. O. (2005) · Current Biology · doi:10.1016/j.cub.2005.06.037 · Cited by 114

A Docking Site in MKK4 Mediates High Affinity Binding to JNK MAPKs and Competes with Similar Docking Sites in JNK Substrates

Ho, D. T., Bardwell, A. J., Abdollahi, M., & Bardwell, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304229200 · Cited by 108

Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity

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Recognition of ERK MAP kinase by PEA‐15 reveals a common docking site within the death domain and death effector domain

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Hydrophobic as Well as Charged Residues in Both MEK1 and ERK2 Are Important for Their Proper Docking

Xu, B.-E., Stippec, S., Robinson, F. L., & Cobb, M. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102769200 · Cited by 91

The cell polarity regulator hScrib controls ERK activation through a KIM site-dependent interaction

Nagasaka, K., Pim, D., Massimi, P., Thomas, M., Tomaić, V, Subbaiah, V. K., Kranjec, C., Nakagawa, S., Yano, T., Taketani, Y., et al. (2010) · Oncogene · doi:10.1038/onc.2010.265 · Cited by 75

Two Clusters of Residues at the Docking Groove of Mitogen-activated Protein Kinases Differentially Mediate Their Functional Interaction with the Tyrosine Phosphatases PTP-SL and STEP

Tárrega, C., Blanco-Aparicio, C., Muñoz, J. J., & Pulido, R. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108874200 · Cited by 33

Quantifying ERK2–protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains

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GCN5–ERK lactylation–phosphorylation loop amplifies lactate-driven cancer progression

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