NPM-ALK-mediated activation of the MAP kinase signaling pathway leads to phosphorylation and activation of MAPK1 (ERK2) (Illert et al, 2012). Nuclear MAPK1 phosphorylates ZC3HC1 at a number of serine residues, with residues 354 and 359 playing an initiating role in subsequent phosphorylations (Illert et al, 2012; Gegenbacher et al, 2019). Phosphorylation of serine residues within ZC3HC1 inactivates the SCF complex, allowing CCNB1 to accumulate and drive entry into mitosis (Ouyang et al, 2003; Basserman et al, 2005; Illert et al, 2012; Gegenbacher et al, 2019). NPM-ALK may also phosphorylate tyrosine residues in ZC3HC1, but the significance of these phosphorylations is not completely elucidated (Ouyang et a, 2003).
Zech, M, Illert, AL, Duyster, J, Moll, C, Bassermann, F, Peschel, C, Kreutmair, S, Albers, C
Duyster, J, von Klitzing, C, Kawaguchi, H, Morris, SW, Bassermann, F, Bai, RY, Peschel, C, Münch, S
Dumit, VI, Lippert, LJ, Duyster, J, Müller-Rudorf, A, Illert, AL, Kreutmair, S, Gräßel, L, Poggio, T, Gengenbacher, A
Duyster, J, von Klitzing, C, Morris, SW, Bassermann, F, Bai, RY, Peschel, C, Klumpen, S, Miething, C, Ouyang, T
protein serine/threonine kinase activity of p-Y185,Y187 MAPK1 dimer [nucleoplasm]
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