Ubiquitination of plasma membrane ectophosphatase in bloodstream forms of Trypanosoma brucei

Bloodstream forms of Trypanosoma brucei contain plasma-membrane-integral acidic ectophosphatase. Here, it is shown by N-terminal sequencing that the ectophosphatase found in ricin-binding material was modified by ubiquitin. Three different ubiquitinated species corresponding to single, double and triple ubiquitinated forms of the enzyme were identified. Immunofluorescence studies with live bloodstream-form parasites showed that the ectophosphatase was localized in the flagellar pocket—the sole site for endocytosis in trypanosomes. As ubiquitin modification of plasma membrane proteins serves as an internalization signal, it is suggested that ubiquitinated ectophosphatase is labelled for endocytosis. This work was supported by the Bundesministerium für Bildung, Wissenschaft, Forschung und Technik, Schwerpunkt für tropenmedizinische Forschung in Heidelberg (01 KA 9301/3).