PKC alpha interacts with and phosphorylates KIT

Stable Identifier
Reaction [transition]
Homo sapiens
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Protein kinase C (PKC) alpha phosphorylates and regulates the activity of several receptor tyrosine kinases including KIT. PKC alpha is involved in a negative feedback loop regulating SCF induced proliferation by phosphorylating and inhibiting the kinase activity of KIT (Blume-Jensen et al. 1994, 1995). PKC alpha phosphorylates KIT on S741 and S746 of the kinase insert (Blume-Jensen et al. 1995). This serine phosphorylation inhibits KIT kinase activity and reduces the capacity of multiple SH2 containing signaling components to associate with KIT (Linnekin 1999).

Literature References
PubMed ID Title Journal Year
7539802 Identification of the major phosphorylation sites for protein kinase C in kit/stem cell factor receptor in vitro and in intact cells

Heldin, CH, Blume-Jensen, P, Rönnstrand, L, Wernstedt, C

J Biol Chem 1995
7520444 Modulation of Kit/stem cell factor receptor-induced signaling by protein kinase C

Waterfield, MD, Heldin, CH, Gout, I, Blume-Jensen, P, Rönnstrand, L

J Biol Chem 1994
Catalyst Activity

protein kinase C activity of PRKCA [cytosol]

Orthologous Events
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