The scaffold protein Cybr is required for cytokine-modulated trafficking of leukocytes in vivo

COPPOLA V, BARRICK CA, BOBISSE S, RODRIGUEZ GALAN MC, PIVETTA M, REYNOLDS D, HOWARD OM, PALKO ME, ESTEBAN PF, YOUNG HA, ROSATO A, TESSAROLLO L

AMER SOC MICROBIOLOGY

Año: 2006 vol. 26 p. 5249 - 5249

span style="font-size: 10pt;"> Trafficking and cell adhesion are key properties of cells of the immune system. However, the molecular pathways that control these cellular behaviors are still poorly understood. Cybr is a scaffold protein highly expressed in the hematopoietic/immune system whose physiological role is still unknown. In vitro studies have shown it regulates LFA-1, a crucial molecule in lymphocyte attachment and migration. Cybr also binds cytohesin-1, a guanine nucleotide exchange factor for the ARF GTPases, which affects actin cytoskeleton remodeling during cell migration. Here we show that expression of Cybr in vivo is differentially modulated by type 1 cytokines during lymphocyte maturation. In mice, Cybr deficiency negatively affects leukocytes circulating