Collapsin response mediator protein 2 (CRMP2) is a well characterized protein. CRMP2 is expressed in several tissues, e.g. in the central nervous system, and is involved in the Semaphorin3A-signalling pathway. In this pathway we focus on the redoxstate of CRMP2. The reduced form enables the polymerization and interconnection of actin via the actin related protein-complex (ARP 2/3 complex). This regulation process of the cytoskeleton triggers axonal outgrowth and cellular interaction and is therefore crucial for neuronal differentiation. In this thesis we aimed at further characterization of CRMP2 in a cellular model of neuronal differentiation. For this purpose we used SH-SY5Y, a dedifferentiated neuronal blastoma cell line, which is well-suited to examine neuronal processes. At first we tested several siRNAs in HeLa cells regarding a post-transcriptional knock-down of CRMP2 in comparison to an unspecific control siRNA. After validation we transfected SH-SY5Y cells with siCRMP2 and siControl. To induce the differentiation into a neuron-like phenotype, we treated the SH-SY5Y cells with all-trans retinoic acid (RS) or dimethyl sulfoxide (DMSO). DMSO was used as control for RS treatment. The morphological and biochemical changes on protein level revealed that the transfection of siCRMP2 in SH-SY5Y cells induces an elongated and more interconnected cell type. Semi-quantitative western blot analyses showed a higher amount of molecules interacting with CasL 1 (MICAL1) in contrast ...