| Summary: | Learning and memory depend on morphological and functional changes to neural spines. Non-muscle
myosin 2b regulates actin dynamics downstream of long-term potentiation induction. However, the
mechanism by which myosin 2b is regulated in the spine has not been fully elucidated. Here, we show that
filamin A-interacting protein (FILIP) is involved in the control of neural spine morphology and is limitedly
expressed in the brain. FILIP bound near the ATPase domain of non-muscle myosin heavy chain IIb, an essential component of myosin 2b, and modified the function of myosin 2b by interfering with its actin-binding activity. In addition, FILIP altered the subcellular distribution of myosin 2b in spines. Moreover, subunits of the NMDA receptor were differently distributed in FILIP-expressing neurons, and
excitation propagation was altered in FILIP-knockout mice. These results indicate that FILIP is a novel, region-specific modulator of myosin 2b.
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