NIPA Defines an SCF-Type Mammalian E3 Ligase that Regulates Mitotic Entry

  title={NIPA Defines an SCF-Type Mammalian E3 Ligase that Regulates Mitotic Entry},
  author={Florian Bassermann and Christine von Klitzing and Silvia M{\"u}nch and Ren-Yuan Bai and Hiroyuki Kawaguchi and Stephan W. Morris and Christian Peschel and Justus Duyster},

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Multisite Phosphorylation of Nuclear Interaction Partner of ALK (NIPA) at G2/M Involves Cyclin B1/Cdk1*♦
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SCF-FBXO31 E3 Ligase Targets DNA Replication Factor Cdt1 for Proteolysis in the G2 Phase of Cell Cycle to Prevent Re-replication*
The data present an additional pathway that contributes to the FBXO31 function as a tumor suppressor and is independent of the pathways previously described for Cdt1 proteolysis in S and G2 phase.
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Oscillating ubiquitination of nuclear cyclin B1 driven by the SCFNIPA complex contributes to the timing of mitotic entry in the mammalian cell cycle.
Regulation of cell cycle drivers by Cullin-RING ubiquitin ligases
This review focuses on how CRLs target key proteins for degradation or otherwise alter their functions to control the progression over the various cell cycle phases leading to cell division and how the anaphase-promoting complex/cyclosome complex closely cooperate to govern efficient cell cycle progression.
PUL21a-Cyclin A2 Interaction is Required to Protect Human Cytomegalovirus-Infected Cells from the Deleterious Consequences of Mitotic Entry
It is concluded that the Cyclin A2-binding function of pUL21a contributes to the maintenance of a cell cycle state conducive for the completion of the HCMV replication cycle.
Deregulated proteolysis by the F-box proteins SKP2 and β-TrCP: tipping the scales of cancer
The functionality and biology of the F-box proteins, SKP2 (S-phase kinase-associated protein 2) and β-TrCP (β-transducin repeat-containing protein), are explored, which are emerging as important players in cancer biogenesis owing to the deregulated proteolysis of their substrates.
Mechanisms and function of substrate recruitment by F-box proteins
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Ubiquitin-dependent degradation of multiple F-box proteins by an autocatalytic mechanism.
  • J. Galan, M. Peter
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1999
The results suggest that ubiquitin-dependent degradation of F-box proteins allows rapid switching among multiple SCF complexes, thereby enabling cells to adapt quickly to changing physiological conditions and progression through different phases of the cell cycle.
Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases.
Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line
It is shown that turnover of phosphorylated cyclin E depends on an SCF-type protein-ubiquitin ligase that contains the human homologue of yeast Cdc4, which is an F-box protein containing repeated sequences of WD40.
Degradation of the SCF component Skp2 in cell-cycle phase G1 by the anaphase-promoting complex
It is shown that the F-box protein Skp2 is polyubiquitinated, and hence earmarked for destruction, by APCCDH1, and accumulation of SCFSKP2 requires prior inactivation of APCC DH1.
Nuclear localization of cyclin B1 mediates its biological activity and is regulated by phosphorylation.
This investigation provides direct evidence for the hypothesis that the control of subcellular localization of cyclins plays a key role in regulating the biological activity of cyclin-dependent kinase-cyclin complexes.
Control of the SCFSkp2–Cks1 ubiquitin ligase by the APC/CCdh1 ubiquitin ligase
The induction of Skp2 and Cks1 degradation in G1 represents a principal mechanism by which APC/CCdh1 prevents the unscheduled degradation of SCFSkp2–Cks1 substrates and maintains the G1 state.