Cybr, a cytokine-inducible protein that binds cytohesin-1 and regulates its activity.

Cytokines regulate lymphocyte development and differentiation, but precisely how they control these processes is still poorly understood. By using microarray technology to detect cytokine-induced genes, we identified a cDNA encoding Cybr, which was increased markedly in cells incubated with IL-2 and IL-12. The mRNA was most abundant in hematopoietic cells ...
and tissues. The predicted amino acid sequence is similar to that of GRP-1-associated protein (GRASP), a recently identified retinoic acid-induced cytohesin-binding protein. Physical interaction, dependent on the coiled-coil domains of Cybr and cytohesin-1, was demonstrated by coimmunoprecipitation of the overexpressed proteins from 293T cells. Cytohesin-1, in addition to its role in cell adhesion, is a guanine nucleotide-exchange protein activator of ARF GTPases. Acceleration of guanosine 5prime prime or minute-O-(thiotriphosphate) binding to ARF by cytohesin-1 in vitro was enhanced by Cybr. Because the binding protein modified activation of ADP ribosylation factor by cytohesin-1, we designate this cytokine-inducible protein Cybr (cytohesin binder and regulator).
Mesh Terms:
Amino Acid Sequence, Animals, Carrier Proteins, Cell Adhesion Molecules, Cell Line, Cloning, Molecular, Gene Expression, Guanine Nucleotide Exchange Factors, Humans, Interleukin-12, Interleukin-2, Membrane Proteins, Mice, Molecular Sequence Data, Proteins, Sequence Homology, Amino Acid, Transcription Factors
Proc. Natl. Acad. Sci. U.S.A.
Date: Mar. 05, 2002
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