Phosphorylation of myosin-V by CaMKII modulates cargo binding, representing a mechanism for regulating organelle transport during mitosis.
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Hypothesis-generating for CaMKII regulation of organelle transport; leaves open relevance to cardiac mitosis in vivo.
Organelle transport by myosin-V is down-regulated during mitosis, presumably by myosin-V phosphorylation. We used mass spectrometry phosphopeptide mapping to show that the tail of myosin-V was phosphorylated in mitotic Xenopus egg extract on a single serine residue localized in the carboxyl-terminal organelle-binding domain. Phosphorylation resulted in the release of the motor from the organelle. The phosphorylation site matched the consensus sequence of calcium/calmodulin-dependent protein kinase II (CaMKII), and inhibitors of CaMKII prevented myosin-V release. The modulation of cargo binding by phosphorylation is likely to represent a general mechanism regulating organelle transport by myosin-V.
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Karcher et al. (2001) studied this question.
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