Filamin A-interacting protein (FILIP) is a region-specific modulator of myosin 2b and controls spine morphology and NMDA receptor accumulation
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...
| Main Authors: | , , , , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2014
|
| Subjects: | |
| Online Access: | http://irep.iium.edu.my/38350/ http://irep.iium.edu.my/38350/ http://irep.iium.edu.my/38350/1/Tariqur.pdf |
| 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. |
|---|