p-Y-JAK1 phosphorylates CSF3R in CSF3 dimer:2xCSF3R:LYN:p-Y-JAK1

Stable Identifier
Reaction [transition]
Homo sapiens
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After JAK1 is phosphorylated and thereby activated in response to CSF3 binding CSF3R, the resulting p-Y-JAK1 phosphorylates tyrosine residues of the cytosolic domain of CSF3R (Nicholson et al. 1994, Shimoda et al. 1997, inferred from mouse homologs). The phosphorylated tyrosine residues of CSF3R then recruit effector proteins such as kinases, STATs, and RAS activators.

Literature References
PubMed ID Title Journal Year
7512720 Tyrosine kinase JAK1 is associated with the granulocyte-colony-stimulating factor receptor and both become tyrosine-phosphorylated after receptor activation

Nicholson, SE, Oates, AC, Harpur, AG, Ziemiecki, A, Wilks, AF, Layton, JE

Proc. Natl. Acad. Sci. U.S.A. 1994
9226159 Jak1 plays an essential role for receptor phosphorylation and Stat activation in response to granulocyte colony-stimulating factor

Shimoda, K, Feng, J, Murakami, H, Nagata, S, Watling, D, Rogers, NC, Stark, GR, Kerr, IM, Ihle, JN

Blood 1997
Catalyst Activity

protein tyrosine kinase activity of CSF3 dimer:2xCSF3R:LYN:p-Y-JAK1 [plasma membrane]

Inferred From
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