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Updated: Apr 20, 2026

Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods
Published on: July 17, 2019
Imbalanced splicing in MAPK signaling sustains Ras-induced transformation
David Müller1, Yvan Martineau1, Corinne Bousquet1
1Inserm UMR-1037, Laboratoire d'excellence Toulouse Cancer: TOUCAN, Équipe labellisée ligue contre le cancer, Université de Toulouse, 31432 Toulouse, France.
Abstract:
Increasingly, evidence suggests that phosphorylation of the mRNA translation initiation factor eIF4E plays an important role in carcinogenesis, downstream of Ras. The eIF4E factor is phosphorylated by MAPK-interacting protein kinases 1 and 2 (MNK1 and MNK2). Due to alternative splicing, two MNK2 proteins exist (MNK2a and MNK2b). While MNK2a possesses a binding site for the stress-induced p38-MAPK, MNK2b does not. Recently, Maimon et al. revealed that a splicing shift towards the MNK2b isoform, in Ras-activated cells, sustains transformation, due to a defect in p38-induced cell death, while the MNK2b-dependent phosphorylation of eIF4E is maintained.
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