Docking interactions in the mitogen-activated protein kinase cascades

Pharmacol Ther. Feb-Mar 2002;93(2-3):193-202. doi: 10.1016/s0163-7258(02)00188-2.


Regulation of cellular functions and responses utilizes a number of the signal transduction pathways. Each pathway should transduce signals with high efficiency and fidelity to avoid unnecessary crosstalks. The mitogen-activated protein kinase (MAPK) cascades regulate a wide variety of cellular functions, including cell proliferation, differentiation, and stress responses. MAPK is activated by MAPK kinase; phosphorylates various targets, including transcription factors and MAPK-activated protein kinases; and is inactivated by several phosphatases. Recent studies have provided a cue to understand the molecular mechanism underlying the signal transduction through the MAPK cascades. In the MAPK cascades, docking interactions, which are achieved through a site outside the catalytic domain of MAPKs, regulate the efficiency and specificity of the enzymatic reactions. The docking interaction is different from a transient enzyme-substrate interaction through the active center. It has been shown that activators, substrates, and inactivators of MAPKs utilize a common site on MAPKs in the docking interaction. Then, the docking interaction may regulate not only the efficiency and specificity of the cascades, but also the ordered and integrated signaling.

Publication types

  • Review

MeSH terms

  • Animals
  • Humans
  • MAP Kinase Signaling System / physiology*
  • Membrane Proteins / physiology*
  • Mitogen-Activated Protein Kinases / classification*
  • Mitogen-Activated Protein Kinases / metabolism
  • Molecular Biology
  • Phosphorylation
  • Signal Transduction / physiology*


  • Membrane Proteins
  • SRPRA protein, human
  • Mitogen-Activated Protein Kinases