RESUMO
The distal pole complex (DPC) assembles signalling proteins at the T cell pole opposite the immunological synapse (IS) and is thought to facilitate T cell activation by sequestering negative regulatory molecules away from the T cell receptor-proximal signalling machinery. Here, we report the translocation of type I protein kinase A (PKA) to the DPC in a fraction of T cells following activation and the localization of type I PKA with known components of the DPC. We propose that sequestration of type I PKA and concomitant loss of cAMP-mediated negative regulation at the IS may be necessary to allow full T cell activation. Moreover, composition of the DPC appears to be modulated by type I PKA activity, as the antagonist Rp-8-Br-cAMPS inhibited translocation of type I PKA and other DPC proteins.
