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Bimolecular fluorescence complementation (BiFC) assay has been proved to be a very useful technique for detecting protein-protein,protein-DNA/RNA,and protein-ligand interactions under physiological or near-physiological conditions [1].The basic strategy of BiFC is to split a fluorescent protein into two non-fluorescent fragments and fuse them to two proteins.When the interactions between these two proteins bring the split fragments into close proximity,the fluorescent protein is reconstituted.Thus,the fluorescence signals can reflect the interactions of the proteins.Here,instead of studying the interactions between two molecules,we report a novel,intra-molecular application of fluorescence complementation assay in studying the topology of proteins with multi-transmembrane domains (TMDs) in living cells.