sigh...英语退步得如此厉害
In the paper about Myosin-X, the author demonstrated that the Myo10(Myosin-X) can directly interact with integrin and mediate its relocalization in the elongation of filopodia by several elaborately devised experiments.
Firstly the author identified Myo10 as a strong and specific integrin-interacting protein, and verified this result by several different approaches. They found the FERM domain of Myo10 played a major role in the protein-protein interaction, and both of the lobes F2 and F3 seem to be required. They also identified NPXY motif and the conserved tryptophan at the -8 position of it as the Myo10-binding region within the integrin.
Secondly, once having observed there was a relationship between overexpression of Myo10 and extension of filopodia, and having demonstrated the interaction between Myo10 and integrin, they continued to determine whether this effect is mediated by integrin. Here, again they set up several precise experiments to observe whether the interaction between Myo10 and integrin played a part in the extension of filopodia. The results supported the proposal that the My10 did effect the function of intergrin and the extension, adhesion and retraction by relocalization and stabilization of integrin to the tips of the filopodia.
The results of this article indicate some potential roles that the integrin may play in some physiological processes, disruption of which may cause some fatal diseases. Since there are large number of myosin or other proteins which may contain a FERM domain, the effects or functions of integrin will be affected by this or that factor, and the consequence becomes hard to predict. So the results of this paper imply further investigation about the other possible function or effect of integrin.
In the paper about Myosin-X, the author demonstrated that the Myo10(Myosin-X) can directly interact with integrin and mediate its relocalization in the elongation of filopodia by several elaborately devised experiments.
Firstly the author identified Myo10 as a strong and specific integrin-interacting protein, and verified this result by several different approaches. They found the FERM domain of Myo10 played a major role in the protein-protein interaction, and both of the lobes F2 and F3 seem to be required. They also identified NPXY motif and the conserved tryptophan at the -8 position of it as the Myo10-binding region within the integrin.
Secondly, once having observed there was a relationship between overexpression of Myo10 and extension of filopodia, and having demonstrated the interaction between Myo10 and integrin, they continued to determine whether this effect is mediated by integrin. Here, again they set up several precise experiments to observe whether the interaction between Myo10 and integrin played a part in the extension of filopodia. The results supported the proposal that the My10 did effect the function of intergrin and the extension, adhesion and retraction by relocalization and stabilization of integrin to the tips of the filopodia.
The results of this article indicate some potential roles that the integrin may play in some physiological processes, disruption of which may cause some fatal diseases. Since there are large number of myosin or other proteins which may contain a FERM domain, the effects or functions of integrin will be affected by this or that factor, and the consequence becomes hard to predict. So the results of this paper imply further investigation about the other possible function or effect of integrin.
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