Conclusions
km23 is a novel motor receptor found to be linked to a TGFβ signaling pathway. Based upon our observations, we have constructed the following model (Fig. 3). Upon phosphorylation of km23 by TβRs, DIC is recruited to form a motor complex. This complex transports membrane vesicles containing TGFβ signaling components such as Smad2 along the microtubules to a new vesicular compartment. After reaching the new compartment, the Smad complex may be translocated to the nucleus for transcriptional regulation of target genes. At this time point, km23 is no longer co-localized with Smad2. Future studies are still required to answer several questions about this novel TGFβ signaling intermediate. For example, we would like to identify other cargoes that km23 carries along the MTs. In addition, it would be of interest to know precisely which serine residues are phosphorylated by TGFβ, as well as what the consequences of dephosphorylation of these sites may be. Overall, we would like to develop km23-based cancer diagnostics and therapeutics, since km23 is altered at such a high rate in ovarian cancer. km23 most likely plays an important role in tumorgenesis or tumor progression in at least this type of cancer. Future studies will reveal whether this is the case for other tumor types as well.
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Ding, W., Mulder, K.M. (2004). km23: A Novel TGFβ Signaling Target Altered in Ovarian Cancer. In: Kumar, R. (eds) Molecular Targeting and Signal Transduction. Cancer Treatment and Research, vol 119. Springer, Boston, MA. https://doi.org/10.1007/1-4020-7847-1_15
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