Interleukin-2 Receptor β Chain Gene: Generation of Three Receptor Forms by Cloned Human α and β Chain cDNA's

Abstract

Interleukin-2 (IL-2) binds to two distinct receptor molecules, the IL-2 receptor alpha (IL-2R alpha, p55) chain and the newly identified IL-2 receptor beta (IL-2R beta, p70-75) chain. The cDNA encoding the human IL-2R beta chain has now been isolated. The overall primary structure of the IL-2R beta chain shows no apparent homology to other known receptors. Unlike the IL-2R alpha chain, the IL-2R beta chain has a large cytoplasmic region in which a functional domain (or domains) mediating an intracellular signal transduction pathway (or pathways) may be embodied. The cDNA-encoded beta chain binds and internalizes IL-2 when expressed on T lymphoid cells but not fibroblast cells. Furthermore, the cDNA gives rise to the generation of high-affinity IL-2 receptor when co-expressed with the IL-2R alpha chain cDNA.

Small-Molecule Inhibitors of IL-2/IL-2R: Lessons Learned and Applied

“…The IL-2 receptor family comprises three single-pass transmembrane proteins, IL-2Ra (p55, CD25), IL-2Rb (p75, CD122), and IL-2Rg (p64, CD132) (Robb et al 1981(Robb et al , 1984bLeonard et al 1984Leonard et al , 1985Greene et al 1986;Hatakeyama et al 1989;Tsudo et al 1990;Takeshita et al 1992;Noguchi et al 1993). IL-2Ra is present at low concentrations on T cells and is expressed along with IL-2 following TCR activation, forming a transient autocrine/paracrine signaling loop.…”

The role of Stat5a and Stat5b in signaling by IL-2 family cytokines

“…This then leads to the recruitment and activation of the signaling molecules associated with IL-2Rb and g c , thereby initiating the IL-2 signaling cascade (Lin and Leonard, 1997) (Figure 2). As is typical of type I cytokine receptors, neither IL-2Rb nor g c contains protein kinase activity in its cytoplasmic domain (Hatakeyama et al, 1989;Takeshita et al, 1992). However, within minutes following the interaction of IL-2 with the high-or intermediate-a nity IL-2 receptors, a number of cellular proteins, including IL2Rb and g c , are phosphorylated on tyrosine residues (Farrar and Ferris, 1989;Turner et al, 1991), at least in part by the receptor-associated protein tyrosine kinases, Jak1 and Jak3 (Friedmann et al, 1996;Johnston et al, 1994;Witthuhn et al, 1994).…”

Bcl-2 differentially targets K-, N-, and H-Ras to mitochondria in IL-2 supplemented or deprived cells: Implications in prevention of apoptosis

“…Interleukin 2 (IL-2) is a regulator of cell cycle progression in T lymphocytes, which binds to a speci®c cell surface receptor (Hatakeyama et al, 1989;Takeshita et al, 1992). IL-2 withdrawal triggers an active cell death program in lymphokine-dependent cells (Go mez et al, 1996(Go mez et al, , 1997Broome et al, 1995a,b;Miyazaki et al, 1995).…”