X-linked and cellular IAPs modulate the stability of C-RAF kinase and cell motility

@article{Dogan2008XlinkedAC,
  title={X-linked and cellular IAPs modulate the stability of C-RAF kinase and cell motility},
  author={Taner Dogan and Gregory S. Harms and Mirko Hekman and Christiaan Karreman and Tripat Kaur Oberoi and Emad S Alnemri and Ulf R{\"u}diger Rapp and Krishnaraj Rajalingam},
  journal={Nature Cell Biology},
  year={2008},
  volume={10},
  pages={1447-1455}
}
Inhibitor of apoptosis proteins (IAP) are evolutionarily conserved anti-apoptotic regulators. C-RAF protein kinase is a direct RAS effector protein, which initiates the classical mitogen-activated protein kinase (MAPK) cascade. This signalling cascade mediates diverse biological functions, such as cell growth, proliferation, migration, differentiation and survival. Here we demonstrate that XIAP and c-IAPs bind directly to C-RAF kinase and that siRNA-mediated silencing of XIAP and c-IAPs leads… 

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X‐linked IAP (XIAP) and cellular IAP1 (c‐IAP1) directly bind to Rac1 in a nucleotide‐independent manner to promote its polyubiquitination at Lys147 and proteasomal degradation, unveiling an evolutionarily conserved role of IAPs in controlling Rac1 stability thereby regulating the plasticity of cell migration and morphogenesis.

The ubiquitin ligase HERC1 regulates cell migration via RAF-dependent regulation of MKK3/p38 signaling

It is shown that the ubiquitin ligase HERC1 regulates the p38 signaling pathway, and that this regulation is mediated by the MAPK kinase MKK3, and a crosstalk between RAF/MKK3/p38 signaling pathways during cell migration is demonstrated.

Characterizing the interaction between RanBPM and c-Raf

It is shown that the N-terminus, LisH/CTLH and CRA domains of RanBPM are required for downregulation of c-Raf and that RanB PM interacts directly with c- Raf through its CRA domain, and that MAEA, another CTLH complex member, associates with c -Raf.
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