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- W1508032932 abstract "This chapter discusses the concepts and experimental approaches to assess the biochemical properties of MEK (MAPK/ERK kinase)-partner 1(MP1). The structural and biochemical properties of MP1 are consistent with it functioning as a molecular scaffold in the extracellular signal-regulated kinases (ERK) pathway. First, MP1 binds with striking specificity to MEK1 and ERK1, but not the closely related family members MEK2 and ERK2. The MP1-MEK1 interaction is dependent on sequences within MEK1 previously found to be necessary for efficient in vivo coupling of MEK activity to ERK. MP1 functions as a coactivator for ERK signaling, consistent with its ability to act as a potent coactivator for MEK in vitro reconstitution experiments. The chapter describes the protein-protein interaction of MP 1. A fundamental property of scaffolding proteins is that they interact with the kinases to be regulated. The chapter describes the coimmunoprecipitation assays to investigate such protein-protein interactions. Coimmunoprecipitation assays have been used to establish interactions between MP1 and its binding partners in mammalian cells. Methods for preparing recombinant proteins and assaying MP1 function in reconstitution experiments have been also discussed in the chapter." @default.
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- W1508032932 date "2001-01-01" @default.
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- W1508032932 title "Scaffold protein regulation of mitogen-activated protein kinase cascade" @default.
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- W1508032932 doi "https://doi.org/10.1016/s0076-6879(01)32216-4" @default.
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