The monoclonal antibody M6-7, which recognizes both native and denatured immunopurified M6a antigen, was used in the present immunocytochemical study to localize its corresponding antigen in young rat brain. Strong labelling was observed in the cerebellar molecular layer, which corresponds to heavily stained axon terminals originating from granule cells. The immunodeposit, as observed by electron microscopy, is present only on the cytoplasmic side of the presynaptic membrane and on the membrane of synaptic vesicles. In contrast, the Purkinje cells and their processes are unstained. Stained synapses are also found, although less frequently, in several other cerebral areas. The pattern of staining at these synapses is similar to that observed in the cerebellar molecular layer. It is hypothesized, on the basis of its restricted distribution in certain neuronal endings and its high homology with myelin proteolipids, that the M6a antigen revealed by the M6-7 antibody is probably involved in a specific biological function in these structures.