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...

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Main Authors: 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
Format: Article
Language:English
Published: Nature Publishing Group 2014
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Online Access:http://irep.iium.edu.my/38350/
http://irep.iium.edu.my/38350/
http://irep.iium.edu.my/38350/1/Tariqur.pdf
id iium-38350
recordtype eprints
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
repository_type Digital Repository
institution_category Local University
institution International Islamic University Malaysia
building IIUM Repository
collection Online Access
language English
topic QP Physiology
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
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.
format Article
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
title 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_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_sort filamin a-interacting protein (filip) is a region-specific modulator of myosin 2b and controls spine morphology and nmda receptor accumulation
publisher Nature Publishing Group
publishDate 2014
url http://irep.iium.edu.my/38350/
http://irep.iium.edu.my/38350/
http://irep.iium.edu.my/38350/1/Tariqur.pdf
first_indexed 2023-09-18T20:55:05Z
last_indexed 2023-09-18T20:55:05Z
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