Editors' ChoiceTarget Specificity

Getting Docked

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Science's STKE  26 Mar 2002:
Vol. 2002, Issue 125, pp. tw119
DOI: 10.1126/stke.2002.125.tw119

Many signals are transduced from the cell surface to the nucleus through pathways involving members of the mitogen-activated protein kinase (MAPK) family: ERK, JNK, and p38. Transcription factors are among the substrates phosphorylated by MAPKs, and precise target interaction underlies the generation of correct biological responses. Although a cluster of conserved residues in transcription factor substrates called the docking site (D domain) has been identified, it has not been clear whether it imparts MAPK specificity. Barsyte-Lovejoy et al. have analyzed the D domains of certain transcription factors and found that their differing responses to alternative MAPKs are determined by submotifs within the D domain. Alanine mutations were generated throughout the D domains, and proficiency of phosphorylation by MAPKs was determined. Three short regions within the D- domain, a basic region, an LXL motif, and a hydrophobic triplet, either promoted or blocked phosphorylation by the three MAPKs.

D. Barsyte-Lovejoy, A. Galanis, A. D. Sharrock, Specificity determinant in MAPK signaling to transcription factors. J Biol. Chem. 277, 9896-9903 (2002). [Abstract] [Full Text]

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