Journal
BIOCHEMISTRY
Volume 53, Issue 2, Pages 350-360Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi401236c
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Funding
- National Natural Science Foundation of China [31071973]
- National Basic Research Program of China [2012CB114102]
- State Key Laboratory of Integrated Management of Pest Insects and Rodents [Chinese IPM1302]
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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.
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