Docking sites on substrate proteins direct extracellular signal - regulated kinase ( ERK ) to phosphorylate specific residues

نویسندگان

  • Douglas A. Fantz
  • Dave Jacobs
  • Danielle Glossip
  • Kerry Kornfeld
  • Dwight Towler
  • Raphael Kopan
  • Mark Sands
  • Jamie Waggoner
  • Edward Mallinckrodt
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Docking sites on substrate proteins direct extracellular signal-regulated kinase to phosphorylate specific residues.

Mitogen-activated protein (MAP) kinases such as extracellular signal-regulated kinase (ERK) are important signaling proteins that phosphorylate (S/T)P sites in many different protein substrates. ERK binding to substrate proteins is mediated by docking sites including the FXFP motif and the D-domain. We characterized the sequence of amino acids that can constitute the FXFP motif using peptide an...

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Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity.

Mitogen-activated protein kinase (MAPK) cascades control gene expression patterns in response to extracellular stimuli. MAPK/ERK (extracellular-signal-regulated kinase) kinases (MEKs) activate MAPKs by phosphorylating them; activated MAPKs, in turn, phosphorylate target transcription factors, and are deactivated by phosphatases. One mechanism for maintaining signal specificity and efficiency is...

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Multiple docking sites on substrate proteins form a modular system that mediates recognition by ERK MAP kinase.

MAP kinases phosphorylate specific groups of substrate proteins. Here we show that the amino acid sequence FXFP is an evolutionarily conserved docking site that mediates ERK MAP kinase binding to substrates in multiple protein families. FXFP and the D box, a different docking site, form a modular recognition system, as they can function independently or in combination. FXFP is specific for ERK,...

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تاریخ انتشار 2001