Phosphorylation of IL2RB Y338, Y392 or Y510 enables STAT recruitment

Stable Identifier
R-HSA-452108
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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Mutation analysis has shown that Y338, Y392 and Y510 are involved in IL-2-induced STAT protein binding. Phospho-tyrosines 338, 392 and 510 can each promote STAT5 activation (Gaffen et al. 1996), though Y510 appears to be the primary site for STAT5 binding (Gesbert et al. 1998). STAT3 may also be recruited to phospho-tyrosines on IL2RB and studies have shown defective IL-2 responses in STAT3-/- T cells, thereby supporting a functional role for STAT3 downstream of IL-2 signaling (Akaishi et al. 1998).

Literature References
PubMed ID Title Journal Year
8702919 Distinct tyrosine residues within the interleukin-2 receptor beta chain drive signal transduction specificity, redundancy, and diversity

Gaffen, SL, Lai, SY, Ha, M, Liu, X, Hennighausen, L, Greene, WC, Goldsmith, MA

J Biol Chem 1996
8631883 Cloning of human Stat5B. Reconstitution of interleukin-2-induced Stat5A and Stat5B DNA binding activity in COS-7 cells

Lin, JX, Mietz, J, Modi, WS, John, S, Leonard, WJ

J Biol Chem 1996
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