The lymphocyte receptor CD6 interacts with syntenin-1, a scaffolding protein containing PDZ domains

摘要: CD6 is a type I membrane glycoprotein expressed on thymocytes, mature T and B1a lymphocytes, CNS cells. binds to activated leukocyte cell adhesion molecule (CD166), considered as costimulatory involved in lymphocyte activation thymocyte development. Accordingly, partially associates with the TCR/CD3 complex colocalizes it at center of immunological synapse (IS) lymphocytes. However, signaling pathway used by still mostly unknown. The yeast two-hybrid system has allowed us identification syntenin-1 an interacting protein cytoplasmic tail CD6. Syntenin-1 PDZ (postsynaptic density protein-95, postsynaptic discs large, zona occludens-1) domain-containing protein, which functions adaptor able bind cytoskeletal proteins signal transduction effectors. Mutational analyses showed that certain amino acids most C-terminal sequence (-YDDISAA) two occludens-1 domains are relevant interaction. Further confirmation CD6-syntenin-1 interaction was obtained from pull-down coimmunoprecipitation assays mammalian Image also accumulates caps IS. Therefore, we propose may function scaffolding coupling likely other receptors cytoskeleton and/or effectors during IS maturation.