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Sci. STKE, 26 April 2005 REVIEWSUbiquitin Chains in the Ladder of MAPK SignalingSignal Transduction Program, The Burnham Institute, La Jolla, CA 92037, USA. Gloss: Cellular responses to stress are regulated by stress-activated protein kinases that are part of the mitogen-activated protein kinase (MAPK) family. Because each component in this signaling cascade has multiple downstream targets, key questions pertaining to the regulation of the stress response include understanding of the mechanisms underlying the duration of their activity, diversification of the signal to select downstream targets, and magnitude of the signal. Here, we summarize our current understanding of ubiquitin’s roles in dictating the type, strength, and specificity of MAPK signaling. Our summary suggests that ubiquitin serves as a key regulator of MAPK, an arrangement that may serve as a paradigm for other signal transduction pathways. *To whom correspondence should be addressed. E-mail: ronai{at}burnham.org
Citation: A. Laine, Z. Ronai, Ubiquitin Chains in the Ladder of MAPK Signaling. Sci. STKE 2005, re5 (2005). THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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Science Signaling. ISSN 1937-9145 (pre-2008: Science's STKE. ISSN 1525-8882)
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