Docking domains and substrate-specificity determination for MAP kinases.

Sharrocks AD; Yang SH; Galanis A

doi:10.1016/s0968-0004(00)01627-3

Abstract

Signalling specificity in eukaryotic cells is maintained by several mechanisms. One mechanism by which mitogen-activated protein (MAP) kinases ensure their specificity of action is by interacting with their substrates through docking domains. These docking domains recruit the kinases to the correct substrates and enhance their fidelity and efficiency of action. Additional specificity determinants in the substrates serve to enhance the specificity of substrate phosphorylation by MAP kinases further.

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Docking domains and substrate-specificity determination for MAP kinases.

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Authors

Abstract

Full text links

References

Mitogen-activated protein kinase pathways.

Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways.

The riddle of MAP kinase signaling specificity.

Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals.

Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain.

Stress-activated protein kinases bind directly to the delta domain of c-Jun in resting cells: implications for repression of c-Jun function.

The regulation of AP-1 activity by mitogen-activated protein kinases.

Transcription factor ATF2 regulation by the JNK signal transduction pathway.

ATF-2 contains a phosphorylation-dependent transcriptional activation domain.

The Elk-1 ETS-domain transcription factor contains a mitogen-activated protein kinase targeting motif.

Citations & impact

Impact metrics

Citations of article over time

Alternative metrics

Article citations

Targeting ERK-MYD88 interaction leads to ERK dysregulation and immunogenic cancer cell death.

Preso enhances mGluR1-mediated excitotoxicity by modulating the phosphorylation of mGluR1-Homer1 complex and facilitating an ER stress after traumatic brain injury.

MAPK-dependent control of mitotic progression in S. pombe.

An Update on Protein Kinases as Therapeutic Targets-Part II: Peptides as Allosteric Protein Kinase C Modulators Targeting Protein-Protein Interactions.

Genome-wide identification and characteristic analysis of ETS gene family in blood clam Tegillarca granosa.

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