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The Zinc-coordinating LIM domain only protein (ZLIM) encoded by the mouse ZLIM gene is closely related to the band 4.2 protein. The protein is highly conserved in evolution, and is known to be associated with actin cytoskeleton of muscle cells and the nuclear membrane of non-muscle cells. Recently, a novel homolog of the ZLIM family, designated DRGZL, has been identified. However, the function of DRGZL is unknown. Here we report the characterization of DRGZL, and demonstrate that DRGZL is localized in both nuclear and cytoplasmic compartments and is associated with the nuclear membrane. Moreover, DRGZL forms a complex with myosin IIa in the nuclear membrane. Interestingly, the myosin light chain kinase (MLCK)-induced phosphorylation at S447 in the DRGZL results in translocation of DRGZL from the nuclear membrane to cytoplasmic compartments. The phosphorylated DRGZL accumulates in the nucleus and decreases the association of DRGZL with myosin IIa. Taken together, the results suggest that phosphorylation of DRGZL at S447 may be involved in intracellular trafficking of DRGZL.Social:

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