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: | , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Publishing Group
2014
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| Online Access: | http://irep.iium.edu.my/38350/ http://irep.iium.edu.my/38350/1/Tariqur.pdf |
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| author | Yagi, Hideshi Nagano, Takashi Xie, Min-Jue Ikeda, Hiroshi Kuroda, Kazuki Komada, Munekazu Iguchi, Tokuichi Rahman, Mohammad Tariqur Morikubo, Soichi Noguchi, Koichi Murase, Kazuyuki Okabe, Masaru Sato, Makoto |
| author_facet | Yagi, Hideshi Nagano, Takashi Xie, Min-Jue Ikeda, Hiroshi Kuroda, Kazuki Komada, Munekazu Iguchi, Tokuichi Rahman, Mohammad Tariqur Morikubo, Soichi Noguchi, Koichi Murase, Kazuyuki Okabe, Masaru Sato, Makoto |
| author_sort | Yagi, Hideshi |
| building | IIUM Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-14T15:51:58Z |
| format | Article |
| id | iium-38350 |
| institution | International Islamic University Malaysia |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-14T15:51:58Z |
| publishDate | 2014 |
| publisher | Nature Publishing Group |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | iium-383502018-06-11T07:00:32Z http://irep.iium.edu.my/38350/ Filamin A-interacting protein (FILIP) is a region-specific modulator of myosin 2b and controls spine morphology and NMDA receptor accumulation Yagi, Hideshi Nagano, Takashi Xie, Min-Jue Ikeda, Hiroshi Kuroda, Kazuki Komada, Munekazu Iguchi, Tokuichi Rahman, Mohammad Tariqur Morikubo, Soichi Noguchi, Koichi Murase, Kazuyuki Okabe, Masaru Sato, Makoto QP Physiology 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. Nature Publishing Group 2014-09 Article PeerReviewed application/pdf en http://irep.iium.edu.my/38350/1/Tariqur.pdf Yagi, Hideshi and Nagano, Takashi and Xie, Min-Jue and Ikeda, Hiroshi and Kuroda, Kazuki and Komada, Munekazu and Iguchi, Tokuichi and Rahman, Mohammad Tariqur and Morikubo, Soichi and Noguchi, Koichi and Murase, Kazuyuki and Okabe, Masaru and Sato, Makoto (2014) Filamin A-interacting protein (FILIP) is a region-specific modulator of myosin 2b and controls spine morphology and NMDA receptor accumulation. Scientific Reports, 4 (6353). pp. 1-13. ISSN 2045-2322 http://www.nature.com/srep/2014/140815/srep06353/full/srep06353.html#affil-auth |
| spellingShingle | QP Physiology Yagi, Hideshi Nagano, Takashi Xie, Min-Jue Ikeda, Hiroshi Kuroda, Kazuki Komada, Munekazu Iguchi, Tokuichi Rahman, Mohammad Tariqur Morikubo, Soichi Noguchi, Koichi Murase, Kazuyuki Okabe, Masaru Sato, Makoto Filamin A-interacting protein (FILIP) is a region-specific modulator of myosin 2b and controls spine morphology and NMDA receptor accumulation |
| title | Filamin A-interacting protein (FILIP) is a region-specific modulator of myosin 2b and controls spine morphology and NMDA receptor accumulation |
| title_full | Filamin A-interacting protein (FILIP) is a region-specific modulator of myosin 2b and controls spine morphology and NMDA receptor accumulation |
| title_fullStr | Filamin A-interacting protein (FILIP) is a region-specific modulator of myosin 2b and controls spine morphology and NMDA receptor accumulation |
| title_full_unstemmed | Filamin A-interacting protein (FILIP) is a region-specific modulator of myosin 2b and controls spine morphology and NMDA receptor accumulation |
| title_short | Filamin A-interacting protein (FILIP) is a region-specific modulator of myosin 2b and controls spine morphology and NMDA receptor accumulation |
| title_sort | filamin a-interacting protein (filip) is a region-specific modulator of myosin 2b and controls spine morphology and nmda receptor accumulation |
| topic | QP Physiology |
| url | http://irep.iium.edu.my/38350/ http://irep.iium.edu.my/38350/ http://irep.iium.edu.my/38350/1/Tariqur.pdf |