Drosophila Myosin-XX Functions as an Actin-Binding Protein To Facilitate the Interaction between Zyx102 and Actin
Drosophila Myosin-XX Functions as an Actin-Binding Protein To Facilitate the Interaction between Zyx102 and Actin
复制标题
果蝇肌球蛋白-XX 作为肌动蛋白结合蛋白发挥作用,促进 Zyx102 和肌动蛋白之间的相互作用。
DOI:
10.1021/bi401236c
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发表时间:
2014-01-21
期刊:
影响因子:
2.9
通讯作者:
Li, Xiang-dong
中科院分区:
文献类型:
--
作者:
Cao, Yang;White, Howard D.;Li, Xiang-dong
The class XX myosin is a member of the diverse myosin superfamily and exists in insects and several lower invertebrates. DmMyo20, the class XX myosin in Drosophila, is encoded by dachs, which functions as a crucial downstream component of the Fat signaling pathway, influencing growth, affinity, and gene expression during development. Sequence analysis shows that DmMyo20 contains a unique extension, the motor domain, followed by one IQ Motif, and a C-terminal tail. To investigate the biochemical. properties of DmMyo20, we expressed several DmMyo20 truncated constructs containing the motor domain in the baculovirus/Sf9 system. We found that the motor domain of DmMyo20 had neither ATPase activity nor the ability to bind to ATP, suggesting that DmMyo20 does not function as a molecular motor. We found that the motor domain of DmMyo20 could specifically bind to actin filaments in an ATP-independent manner and enhance the interaction between actin filaments and Zyx102, a downstream component of DmMyo20 in the Fat signaling pathway. These results suggest that DmMyo20 functions as a scaffold protein, but not as a molecular motor, in a signaling pathway controlling cell differentiation.