Abstract
The plasma membrane (PM) tension has emerged as a key regulator for fundamental cellular functions. However, a missing link between PM tension and biochemical reaction precludes our understanding of how PM tension is coupled to cellular events like directed migration. We found that FBP17, an F-BAR domain protein, acts as a membrane tension sensor that organizes cell polarity during cell migration. The mechanism is based on membrane-bending activity of the F-BAR domain that is counteracted by PM tension. Because FBP17 binds and activates WASP/N-WASP to promote actin polymerization, it corresponds to the local activator of actin polymerization in the feedback loop regulated by PM tension for self-organized formation of the leading edge. These findings provide an important mechanistic insight into cell migration underpinning a wide variety of physiological events such as development, immune response, and cancer metastasis.
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