Evidence map›Paper›PMID 25220605›Full record

ArticleScientific reports2014

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

Hideshi Yagi, Takashi Nagano, Min-Jue Xie, Hiroshi Ikeda, Kazuki Kuroda, Munekazu Komada, Tokuichi Iguchi, Rahman M Tariqur, Soichi Morikubo, Koichi Noguchi and 3 more

Abstract read
In one paragraph

Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

8 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Hideshi Yagi1] 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.
Takashi NaganoDivision of Cell Biology and Neuroscience, Department of Morphological and Physiological Sciences, Faculty of Medical Sciences, University of Fukui, Fukui 910-1193, Japan.
Min-Jue Xie1] 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.
Hiroshi Ikeda1] 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.
Kazuki Kuroda1] 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.
Munekazu Komada1] 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.
Tokuichi Iguchi1] 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.
Rahman M TariqurDivision of Cell Biology and Neuroscience, Department of Morphological and Physiological Sciences, Faculty of Medical Sciences, University of Fukui, Fukui 910-1193, Japan.
Soichi Morikubo1] 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.
Koichi NoguchiDepartment of Anatomy and Neuroscience, Hyogo College of Medicine, Hyogo 663-8501, Japan.
Kazuyuki Murase1] 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.
Masaru OkabeDepartment of Experimental Genome Research, Genome Information Research Center, Osaka University, Osaka 565-0871, Japan.
Makoto Sato1] 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.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

ActinsAnimalsBlotting, WesternCarrier ProteinsCells, CulturedDendritic SpinesImmunoenzyme TechniquesImmunoprecipitationLong-Term PotentiationMiceMice, Inbred ICRMice, KnockoutMyosin Heavy ChainsNeuronsNonmuscle Myosin Type IIBProtein BindingActinsCarrier ProteinsFILIP protein, mouseMyosin Heavy ChainsNonmuscle Myosin Type IIBnonmuscle myosin type IIB heavy chainReceptors, N-Methyl-D-Aspartate

Identifiers

PMID25220605
PMCPMC4163676

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.