Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Sci. STKE, 26 March 2002
Vol. 2002, Issue 125, p. tw119
[DOI: 10.1126/stke.2002.125.tw119]


Target Specificity Getting Docked

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]

Citation: Getting Docked. Sci. STKE 2002, tw119 (2002).

To Advertise     Find Products

Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882