Correlation Engine 2.0
Clear Search sequence regions


  • ASK1 (1)
  • cellular (1)
  • cellular processes (1)
  • DLK1 (1)
  • enzymes (5)
  • ERK1 (2)
  • ERK5 (1)
  • humans (1)
  • JNK1 (1)
  • MAPK (5)
  • mapk p38 (1)
  • MAPKK (3)
  • MEK1 2 (1)
  • MEKK1 4 (1)
  • MEKK2 (1)
  • mitogen (1)
  • mono (1)
  • proteins ubiquitin (1)
  • signal (1)
  • TAK1 (1)
  • ubiquitin (4)
  • ubiquitin protein ligases (2)
  • Sizes of these terms reflect their relevance to your search.

    The mitogen-activated protein kinase (MAPK) signaling pathway is the primary regulatory module of various cellular processes such as cell proliferation, differentiation, and stress responses. This pathway converts external stimuli to cellular responses via three major kinases: mitogen-activated protein kinase (MAPK), mitogen-activated protein kinase kinase (MAPKK), and mitogen-activated protein kinase kinase kinase (MAPKKK). Ubiquitination is a post-translational modification of proteins with ubiquitin, which results in the formation of mono- or poly-ubiquitin chains of substrate proteins. Conversely, removal of the ubiquitin by deubiquitinating enzymes (DUBs) is known as deubiquitination. This review summarizes mechanisms of the MAPK signaling pathways (ERK1/2, ERK5, p38, and JNK1/2/3 signaling pathway) in cancers, and of E3 ligases and DUBs that target the MAPK signaling components such as Raf, MEK1/2, ERK1/2, MEKK2/3, MEKK1-4, TAK1, DLK1, MLK1-4, ASK1/2, and MKK3-7. Copyright © 2022 Elsevier B.V. All rights reserved.

    Citation

    Hong-Beom Park, Kwang-Hyun Baek. E3 ligases and deubiquitinating enzymes regulating the MAPK signaling pathway in cancers. Biochimica et biophysica acta. Reviews on cancer. 2022 May;1877(3):188736

    Expand section icon Mesh Tags

    Expand section icon Substances


    PMID: 35589008

    View Full Text