Critical processes such as cell division and differentiation depend on correct protein localization [4], [5], yet for most localized proteins the mechanisms responsible for localization are unknown.
The mechanism behind this heterogeneous localization is unknown.
However, the mechanism of this localization is unknown.
Unfortunately, the mechanism of p38 MAPK nuclear localization is unknown (p38 MAPKs, including PMK-3, lack a consensus nuclear localization signal), precluding us from conducting such a test [51].
How the Ft-Ds-Fj system might generate cellular asymmetries that regulate Dachs localization is unknown.
We intend to apply this method to predict subcellular localizations in other organisms in which the true localization is unknown.
Interestingly, mature miR-206 has been reported to have both nuclear localization and cytosolic localization but the functional relevance of compartmentalized localization is unknown.
Unfortunately, for a majority of these proteins their subcellular localization is unknown and experimentally determining the localization of a protein is expensive and time-consuming.
Interestingly, the Rad54 homolog, Rdh54, is recruited both to DSBs and to the kinetochore, although the functional significance of this dual localization is unknown.
In the case of zebrafish RNase Dre1 and RNase Dre2 the localization is unknown, but subcellular localization predictions using different programs (see Material and Methods) indicate either extracellular or microsomal/lysosomal localization, almost identical to predictions for the human enzyme.
