From a human dendritic cell (DC) cDNA library, we identified a novel type I cytokine receptor, designated as cytokine receptor-like molecule 2 (CRL2). CRL2 cDNA encoded a 371-residue type I transmembrane protein with an extracellular domain of 210 residues and an intracellular domain of 119 residues. Its extracellular domain contains conserved cysteine residues and WAS-like motif in place of the hallmark of WSXWS motif present in other type I cytokine receptors. The intracellular domain contained a membrane-proximal "box 1" motif and conserved tyrosine residue potentially as a binding site for signal transducing molecules. CRL2 protein shares significant homology with common cytokine receptor (gammac) and interleukin-13 receptor alpha1 chain. Northern blot analysis showed that CRL2 was restrictedly expressed by spleen and peripheral blood leukocytes, and abundantly expressed by HL-60 cells. RT-PCR analysis demonstrated that CRL2 was preferentially expressed by DC and monocytes. Interestingly, CRL2 expression was up-regulated when monocytes were activated by LPS. These indicate that CRL2 may be involved in the biological functions of DC and monocytes. The Ba/F3 transfectants of CRL2 was retrovirally established with the expressed FLAG-tagged CRL2 in the size of approximately 48 kD, which could be efficiently immunoprecipitated. We also prepared a CRL2Ig fusion protein. The identification of its ligand and involvement of signal transduction will help to elucidate its potential function.
Copyright 2001 Academic Press.