We therefore undertook studies that aimed to explore the Fenticonazole Nitrate nuclear expression of SEDLIN, which would be consistent with its interactions with the transcription factors MBP1, PITX1 and SF1, and to determine the functional consequences of disease-associated SEDLIN mutations on the subcellular localization and interactions with PITX1, MBP1 and SF1. We focused on the 4 SEDT-associated missense mutations as these were predicted to yield a full-length protein and were not Cinacalcet likely to affect the tertiary structure of SEDLIN substantially, as well as the most C-terminal nonsense mutation, which if translated, is predicted to result in the loss of the last ten amino acids. Our results show that SEDLIN forms homodimers, is localized to the cytoplasm and nucleus, and that wild-type SEDLIN co-localizes and interacts with the transcription factors MBP1, PITX1 and SF1. In addition, our results show that SEDT-associated SEDLIN mutations do not result in abnormalities of subcellular localization, but those involving residues within the hydrophobic core do lead to a loss of interactions with the transcription factors MBP1, PITX1 and SF1. The relevance and further insights provided by these findings may help to elucidate the role of SEDLIN in cellular functions. The dimerization of SEDLIN and its nuclear localization points to additional roles for mammalian SEDLIN, which with its yeast orthologue Trs20p, have previously been reported to be present as monomers in the TRAPP complex, where SEDLIN is involved in tethering vesicles. However, the formation of SEDLIN dimers and their nuclear localization together with the interactions with MBP1, PITX1 and SF1 indicate a role in modulating transcription and the situation may be analogous to that observed with the c-Jun Nterminal kinase -interacting protein 1. The monomeric form of JIP-1 is a cytoplasmic scaffold protein that is essential for the organization of the JNK signalling pathway, while the dimeric form is predominantly located in the nucleus, where it likely mediates transcription control of pathways involved in prevention of neuronal death.