The dimerization of JIP-1 involves Fluoxymesterone post-translation modification and is dependent on phosphorylation, and it is interesting to note that SEDLIN has predicted phosphorylation sites at Ser119 and Ser124. The mechanisms that transport SEDLIN into the nucleus remain to be defined, as SEDLIN does not have a nuclear localization signal. It seems likely that SEDLIN may be co-transported with the interacting proteins that contain NLSs, thereby enabling it to enter the nucleus. Within the nucleus SEDLIN, given its interaction with the transcription factors MBP1, PITX1 and SF1, may act as either a co-repressor or co-activator of gene transcription. For example, SEDLIN acts as a repressor molecule by binding to PITX1 and SF1 and inhibiting transactivation, as well as an activator by binding to repressor molecules such as MBP1 that facilitate gene transcription. The roles of these interactions between SEDLIN and MBP1, PITX1 and SF1 in skeletal biology remain to be elucidated. However, in vitro studies have shown that SEDLIN Fosinopril Sodium inhibits MBP1 mediated repression of cmyc transcription, and MBP1 has been reported to be associated with two different cellular processes during endochondral ossification; cell proliferation in the proliferative and upper hypertrophic layers, and apoptosis in the lower hypertrophic layer of the growth plate. Thus, one possibility may be that the mutant SEDLINs that are associated with SEDT and lead to a loss of interaction with MBP1 may disrupt the tight control between proliferation and apoptosis in endochondral ossification. In addition, SEDLIN has been reported to inhibit the PITX1 and SF1 mediated transactivation of the b-subunit of the luteinizing hormone, and the effects of the loss of interaction, due to the SEDLIN mutations, between SEDLIN and PITX1 and SF1 on the pituitary-gonadal response and the delayed puberty observed in some boys affected with SEDT remain to be defined. The Asp47Tyr SEDT-causing mutation, unlike the Ser73Leu, Phe83Ser, Val130Asp and Gln131Stop mutants, did not result in loss of interaction with MBP1, PITX1 and SF1. However, the Asp47 residue, which is conserved through to yeast, has an important functional role, as in a yeast complementation study, the mutant SEDLIN, Asp47Tyr, failed to rescue the lethal trs20pD phenotype.