KRAS4B, unique among RAS isoforms, has been shown to bind to calmodulin (Villalonga et al, 2001; Lopez-Alcala et al, 2008). This interaction is thought to decrease the affinity of KRAS4B for the plasma membrane (Fivaz and Meyer, 2005; Sidhu et al, 2003; reviewed in Ahearn et al, 2018; Nussinov et al, 2015). Interaction between oncogenic KRAS4B and calmodulin has been shown to promote tumorigenesis by interfering with the activation of CAMK2. This in turn relieves the suppression of beta-catenin dependent signaling mediated by the non-canonical WNT signaling pathway (Wang et al, 2015).The interaction between KRAS4B and calmodulin is inhibited by PKC- or PRKG2-dependent KRAS4B phosphorylation at serine 181 (Wang et al, 2015; Alvarez-Moya et al, 2010; reviewed in Ahearn et al, 2018).
Balmain, A, Galeas, J, Wang, MT, To, MD, McCormick, F, Delrosario, R, Holderfield, M
Lopez-Alcalá, C, Villalonga, P, Alvarez-Moya, B, Agell, N, Calvo, M, Bachs, O
Meyer, T, Fivaz, M
Villalonga, P, Rocamora, N, Bosch, M, Agell, N, Gil, J, López-Alcalá, C, Marshall, CJ, Chiloeches, A, Bachs, O, Marais, R
Philips, MR, Zhou, M, Ahearn, I
Nussinov, R, Jang, H, Keskin, O, Tsai, CJ, Muratcioglu, S, Gursoy, A
Agell, N, López-Alcalá, C, Drosten, M, Bachs, O, Alvarez-Moya, B
Bhullar, RP, Clough, RR, Sidhu, RS
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