MAPK1 phsophorylates ZC3HCF1 in a NPM-ALK-dependent manner

Stable Identifier
R-HSA-9725030
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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).

Literature References
PubMed ID Title Journal Year
22955283 Extracellular signal-regulated kinase 2 (ERK2) mediates phosphorylation and inactivation of nuclear interaction partner of anaplastic lymphoma kinase (NIPA) at G2/M

Zech, M, Illert, AL, Duyster, J, Moll, C, Bassermann, F, Peschel, C, Kreutmair, S, Albers, C

J Biol Chem 2012
16009132 NIPA defines an SCF-type mammalian E3 ligase that regulates mitotic entry

Duyster, J, von Klitzing, C, Kawaguchi, H, Morris, SW, Bassermann, F, Bai, RY, Peschel, C, Münch, S

Cell 2005
31434245 Proteomic Phosphosite Analysis Identified Crucial NPM-ALK-Mediated NIPA Serine and Threonine Residues

Dumit, VI, Lippert, LJ, Duyster, J, Müller-Rudorf, A, Illert, AL, Kreutmair, S, Gräßel, L, Poggio, T, Gengenbacher, A

Int J Mol Sci 2019
12748172 Identification and characterization of a nuclear interacting partner of anaplastic lymphoma kinase (NIPA)

Duyster, J, von Klitzing, C, Morris, SW, Bassermann, F, Bai, RY, Peschel, C, Klumpen, S, Miething, C, Ouyang, T

J Biol Chem 2003
Participants
Participates
Catalyst Activity

protein serine/threonine kinase activity of p-Y185,Y187 MAPK1 dimer [nucleoplasm]

Disease
Name Identifier Synonyms
cancer DOID:162 malignant tumor, malignant neoplasm, primary cancer
Authored
Reviewed
Created
Cite Us!