Alterations in the mitochondrial ultrastructure, primarily alterations in cristae morphology are among other things possible causes for human degenerative diseases. Based on those facts, the influence of the mitochondrial ultrastructure on the cellular Ca2+ homeostasis as well as on the mitochondrial morphology and functions should be examined. To investigate the impact of the mitochondrial ultrastructure on cell signalling, a suitable method for a specific and temporary manipulation of the mitochondrial ultrastructure is aspired. Accordingly, the aim of this work is to establish a novel strategy to link the outer to the inner mitochondrial membrane as well as the mitochondrial cristae membranes with each other. For this purpose, the rapamycin inducible heterodimerisation assay by Rivera was adapted. Therefore constructs, composed of three elements, were synthesized. 1. proteins, which are anchored to the respective mitochondrial membrane such as Translocase of outer mitochondrial membrane 22 (Tom22) and Translocase of inner mitochondrial membrane 50 (Tim50). 2. the heterodimerisation domains of the FK506-binding protein (FKBP) and of the FKBP12-rapamycin-binding (FRB) domain of human mTOR, which interact with each other after stimulation with rapamycin. 3. fluorescent proteins, which allow an assessment of the subcellular localisation of the constructs and the quantitative measurement of dimerisation using fluorescence microscopy. This adapted heterodimerisation assay was successfully established and used concerning cristae linkage.