JIP4 is a PLK1 binding protein that regulates p38MAPK activity in G2 phase
Autor: | Dorothy Loo, Michelle M. Hill, Brian Gabrielli, Alex Pinder, Brittney S. Harrington, Vanessa Oakes |
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Rok vydání: | 2015 |
Předmět: |
G2 Phase
M Phase Cell Cycle Checkpoints Cyclin B Mitosis Cell Cycle Proteins Protein Serine-Threonine Kinases p38 Mitogen-Activated Protein Kinases G2 phase Cell Line Tumor Proto-Oncogene Proteins CDC2 Protein Kinase Humans Biochemical switches in the cell cycle Phosphorylation RNA Small Interfering Adaptor Proteins Signal Transducing biology Chemistry G1/S transition S-phase-promoting factor Cell Biology Cyclin-Dependent Kinases Cell biology Protein Structure Tertiary HEK293 Cells Mitotic exit biology.protein RNA Interference G1 phase HeLa Cells Protein Binding |
Zdroj: | Cellular signalling. 27(11) |
ISSN: | 1873-3913 |
Popis: | Cell cycle progression from G2 phase into mitosis is regulated by a complex network of mechanisms, all of which finally control the timing of Cyclin B/CDK1 activation. PLK1 regulates a network of events that contribute to regulating G2/M phase progression. Here we have used a proteomics approach to identify proteins that specifically bind to the Polobox domain of PLK1. This identified a panel of proteins that were either associated with PLK1 in G2 phase and/or mitosis, the strongest interaction being with the MAPK scaffold protein JIP4. PLK1 binding to JIP4 was found in G2 phase and mitosis, and PLK1 binding was self-primed by PLK1 phosphorylation of JIP4. PLK1 binding is required for JIP4-dependent p38MAPK activation in G2 phase during normal cell cycle progression, but not in either G2 phase or mitotic stress response. Finally, JIP4 is a target for caspase-dependent cleavage in mitotically arrested cells. The role for the PLK1-JIP4 regulated p38MAPK activation in G2 phase is unclear, but it does not affect either progression into or through mitosis. |
Databáze: | OpenAIRE |
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