2. Academic Validation
  3. Filamin A-interacting protein (FILIP) is a region-specific modulator of myosin 2b and controls spine morphology and NMDA receptor accumulation

Filamin A-interacting protein (FILIP) is a region-specific modulator of myosin 2b and controls spine morphology and NMDA receptor accumulation

  • Sci Rep. 2014 Sep 15:4:6353. doi: 10.1038/srep06353.
Hideshi Yagi 1,  Takashi Nagano 2,  Min-Jue Xie 3,  Hiroshi Ikeda 4,  Kazuki Kuroda 3,  Munekazu Komada 3,  Tokuichi Iguchi 5,  Rahman M Tariqur 2,  Soichi Morikubo 6,  Koichi Noguchi 7,  Kazuyuki Murase 4,  Masaru Okabe 8,  Makoto Sato 9
Affiliations

Affiliations

  • 1 1] Division of Cell Biology and Neuroscience, Department of Morphological and Physiological Sciences, Faculty of Medical Sciences, University of Fukui, Fukui 910-1193, Japan [2] Research and Education Program for Life Science, University of Fukui, Fukui 910-8507, Japan [3] Department of Anatomy and Neuroscience, Hyogo College of Medicine, Hyogo 663-8501, Japan.
  • 2 Division of Cell Biology and Neuroscience, Department of Morphological and Physiological Sciences, Faculty of Medical Sciences, University of Fukui, Fukui 910-1193, Japan.
  • 3 1] Division of Cell Biology and Neuroscience, Department of Morphological and Physiological Sciences, Faculty of Medical Sciences, University of Fukui, Fukui 910-1193, Japan [2] Research and Education Program for Life Science, University of Fukui, Fukui 910-8507, Japan.
  • 4 1] Research and Education Program for Life Science, University of Fukui, Fukui 910-8507, Japan [2] Department of Human and Artificial Intelligence Systems, Faculty of Engineering, University of Fukui, Fukui 910-8507, Japan.
  • 5 1] Division of Cell Biology and Neuroscience, Department of Morphological and Physiological Sciences, Faculty of Medical Sciences, University of Fukui, Fukui 910-1193, Japan [2] Research and Education Program for Life Science, University of Fukui, Fukui 910-8507, Japan [3] Department of Anatomy and Neuroscience, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
  • 6 1] Division of Cell Biology and Neuroscience, Department of Morphological and Physiological Sciences, Faculty of Medical Sciences, University of Fukui, Fukui 910-1193, Japan [2] Division of Ophthalmology, Department of Sensory and Locomotor Medicine, Faculty of Medical Sciences, University of Fukui, Fukui 910-1193, Japan.
  • 7 Department of Anatomy and Neuroscience, Hyogo College of Medicine, Hyogo 663-8501, Japan.
  • 8 Department of Experimental Genome Research, Genome Information Research Center, Osaka University, Osaka 565-0871, Japan.
  • 9 1] Division of Cell Biology and Neuroscience, Department of Morphological and Physiological Sciences, Faculty of Medical Sciences, University of Fukui, Fukui 910-1193, Japan [2] Research and Education Program for Life Science, University of Fukui, Fukui 910-8507, Japan [3] Research Center for Child Mental Development, University of Fukui, Fukui 910-1193, Japan [4] United Graduate School of Child Development, Osaka University, Kanazawa University, Hamamatsu University School of Medicine, Chiba University and University of Fukui, Osaka 565-0871, Japan [5] Department of Anatomy and Neuroscience, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
PMID: 25220605 DOI: 10.1038/srep06353
Abstract

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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