The immunohistochemical localization of an endogenous lectin R1 isolated from the rat cerebellum was studied during its postnatal development. The lectin is present in the cerebellum from birth to adulthood, essentially in lysosomes, multivesicular bodies, and parts of the endoplasmic reticulum, principally of large and intermediate size neurons. During the period of massive synaptogenesis in the molecular layer, there is a sprouting of R1 in some distal dendrites of Purkinje cells. The lectin appears to be particularly concentrated on their plasma membranes, in coated pits, in coated vesicles, multivesicular bodies and lysosomes. At the same period, in cerebella of rats treated with chloroquine (an inhibitor of lysosomal function), both the lectin and mannose-rich glycoproteins of newly formed parallel fibres (able to bind specifically this lectin) are found in the same non-functional lysosomes of Purkinje cells. It is thus suggested that both this lectin (with a high-affinity for the glycans of the mannose-rich glycoproteins of the membrane of the newly formed parallel fibres) and these glycoproteins could be the recognition molecules allowing a specific contact between parallel fibres and Purkinje cells at the period of synaptogenesis.