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  1. Article ; Online: Dynamins in human diseases: differential requirement of dynamin activity in distinct tissues.

    Laiman, Jessica / Lin, Shan-Shan / Liu, Ya-Wen

    Current opinion in cell biology

    2023  Volume 81, Page(s) 102174

    Abstract: Dynamin, a 100-kDa GTPase, is one of the most-characterized membrane fission machineries catalyzing vesicle release from plasma membrane during endocytosis. The human genome encodes three dynamins: DNM1, DNM2 and DNM3, with high amino acid similarity but ...

    Abstract Dynamin, a 100-kDa GTPase, is one of the most-characterized membrane fission machineries catalyzing vesicle release from plasma membrane during endocytosis. The human genome encodes three dynamins: DNM1, DNM2 and DNM3, with high amino acid similarity but distinct expression patterns. Ever since the discoveries of dynamin mutations associated with human diseases in 2005, dynamin has become a paradigm for studying pathogenic mechanisms of mutant proteins from the aspects of structural biology, cell biology, model organisms as well as therapeutic strategy development. Here, we review the diseases and pathogenic mechanisms caused by mutations of DNM1 and DNM2, focusing on the activity requirement and regulation of dynamins in different tissues.
    MeSH term(s) Humans ; Dynamin II/genetics ; Dynamin II/metabolism ; Dynamins/genetics ; Mutation ; GTP Phosphohydrolases ; Endocytosis
    Chemical Substances Dynamin II (EC 3.6.5.5) ; Dynamins (EC 3.6.5.5) ; GTP Phosphohydrolases (EC 3.6.1.-)
    Language English
    Publishing date 2023-05-23
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2023.102174
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2963: Show issues Location:
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  2. Article ; Online: Cellular Assays for Measuring Dynamin Activity in Muscle Cells.

    Laiman, Jessica / Liu, Ya-Wen

    Methods in molecular biology (Clifton, N.J.)

    2020  Volume 2159, Page(s) 179–187

    Abstract: Dynamin is one of the best-studied membrane fission machineries, which mediates endocytic vesicle pinch-off from the plasma membrane. Among the three dynamin isoforms encoded in mammalian genome, dynamin-2 is the ubiquitously expressed isoform and leads ... ...

    Abstract Dynamin is one of the best-studied membrane fission machineries, which mediates endocytic vesicle pinch-off from the plasma membrane. Among the three dynamin isoforms encoded in mammalian genome, dynamin-2 is the ubiquitously expressed isoform and leads to human muscular or neuronal diseases when mutants causing hyperactivity or hypoactivity of its membrane fission activity occur. While transferrin uptake is the most commonly used assay to measure dynamin activity in cultured cells, here we provide two different methods to quantitatively examine the activity of dynamin in myoblasts and myotubes, i.e., Bin1-tubule vesiculation and glucose transporter 4 fractionation assays, respectively. These methods could provide a quantitative measurement of dynamin activity in both differentiated and undifferentiated myoblasts.
    MeSH term(s) Animals ; Biomarkers ; Cell Line ; Cells, Cultured ; Dynamins/genetics ; Dynamins/metabolism ; Enzyme Activation ; Enzyme Assays/methods ; Fluorescent Antibody Technique ; Gene Expression ; Glucose Transporter Type 4/metabolism ; Microscopy, Confocal ; Muscle Cells/metabolism ; Myoblasts/metabolism ; Rats ; Transfection
    Chemical Substances Biomarkers ; Glucose Transporter Type 4 ; Dynamins (EC 3.6.5.5)
    Language English
    Publishing date 2020-06-12
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-0676-6_13
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: GSK3α phosphorylates dynamin-2 to promote GLUT4 endocytosis in muscle cells.

    Laiman, Jessica / Hsu, Yen-Jung / Loh, Julie / Tang, Wei-Chun / Chuang, Mei-Chun / Liu, Hui-Kang / Yang, Wei-Shun / Chen, Bi-Chang / Chuang, Lee-Ming / Chang, Yi-Cheng / Liu, Ya-Wen

    The Journal of cell biology

    2022  Volume 222, Issue 2

    Abstract: Insulin-stimulated translocation of glucose transporter 4 (GLUT4) to plasma membrane of skeletal muscle is critical for postprandial glucose uptake; however, whether the internalization of GLUT4 is also regulated by insulin signaling remains unclear. ... ...

    Abstract Insulin-stimulated translocation of glucose transporter 4 (GLUT4) to plasma membrane of skeletal muscle is critical for postprandial glucose uptake; however, whether the internalization of GLUT4 is also regulated by insulin signaling remains unclear. Here, we discover that the activity of dynamin-2 (Dyn2) in catalyzing GLUT4 endocytosis is negatively regulated by insulin signaling in muscle cells. Mechanistically, the fission activity of Dyn2 is inhibited by binding with the SH3 domain of Bin1. In the absence of insulin, GSK3α phosphorylates Dyn2 to relieve the inhibition of Bin1 and promotes endocytosis. Conversely, insulin signaling inactivates GSK3α and leads to attenuated GLUT4 internalization. Furthermore, the isoform-specific pharmacological inhibition of GSK3α significantly improves insulin sensitivity and glucose tolerance in diet-induced insulin-resistant mice. Together, we identify a new role of GSK3α in insulin-stimulated glucose disposal by regulating Dyn2-mediated GLUT4 endocytosis in muscle cells. These results highlight the isoform-specific function of GSK3α on membrane trafficking and its potential as a therapeutic target for metabolic disorders.
    MeSH term(s) Animals ; Mice ; Adaptor Proteins, Signal Transducing ; Dynamin II/metabolism ; Endocytosis ; Glucose ; Glucose Transporter Type 4/metabolism ; Glycogen Synthase Kinase 3/metabolism ; Insulin ; Insulin Resistance ; Muscle Cells/metabolism
    Chemical Substances Adaptor Proteins, Signal Transducing ; Bin1 protein, mouse ; Dynamin II (EC 3.6.5.5) ; Glucose (IY9XDZ35W2) ; Glucose Transporter Type 4 ; Glycogen Synthase Kinase 3 (EC 2.7.11.26) ; Insulin ; Slc2a4 protein, mouse ; DNM2 protein, mouse (EC 3.6.5.5)
    Language English
    Publishing date 2022-11-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.202102119
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Dynamin-2 mutations associated with centronuclear myopathy are hypermorphic and lead to T-tubule fragmentation.

    Chin, Yu-Han / Lee, Albert / Kan, Hung-Wei / Laiman, Jessica / Chuang, Mei-Chun / Hsieh, Sung-Tsang / Liu, Ya-Wen

    Human molecular genetics

    2015  Volume 24, Issue 19, Page(s) 5542–5554

    Abstract: Skeletal muscle requires adequate membrane trafficking and remodeling to maintain its normal structure and functions. Consequently, many human myopathies are caused by mutations in membrane trafficking machinery. The large GTPase dynamin-2 (Dyn2) is best ...

    Abstract Skeletal muscle requires adequate membrane trafficking and remodeling to maintain its normal structure and functions. Consequently, many human myopathies are caused by mutations in membrane trafficking machinery. The large GTPase dynamin-2 (Dyn2) is best known for catalyzing membrane fission during clathrin-mediated endocytosis (CME), which is critical for cell signaling and survival. Despite its ubiquitous expression, mutations of Dyn2 are associated with two tissue-specific congenital disorders: centronuclear myopathy (CNM) and Charcot-Marie-Tooth (CMT) neuropathy. Several disease models for CNM-Dyn2 have been established to study its pathogenic mechanism; yet the cellular and biochemical effects of these mutations are still not fully understood. Here we comprehensively compared the biochemical activities of disease-associated Dyn2 mutations and found that CNM-Dyn2 mutants are hypermorphic with enhanced membrane fission activity, whereas CMT-Dyn2 is hypomorphic. More importantly, we found that the expression of CNM-Dyn2 mutants does not impair CME in myoblast, but leads to T-tubule fragmentation in both C2C12-derived myotubes and Drosophila body wall muscle. Our results demonstrate that CNM-Dyn2 mutants are gain-of-function mutations, and their primary effect in muscle is T-tubule disorganization, which explains the susceptibility of muscle to Dyn2 hyperactivity.
    MeSH term(s) Animals ; Cell Line ; Charcot-Marie-Tooth Disease/genetics ; Charcot-Marie-Tooth Disease/metabolism ; Charcot-Marie-Tooth Disease/pathology ; Clathrin/metabolism ; Drosophila/genetics ; Drosophila/metabolism ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Dynamin II/genetics ; Dynamin II/metabolism ; Endocytosis ; Humans ; Mice ; Muscle, Skeletal/cytology ; Muscle, Skeletal/metabolism ; Mutation ; Myopathies, Structural, Congenital/genetics ; Myopathies, Structural, Congenital/metabolism ; Myopathies, Structural, Congenital/pathology
    Chemical Substances Clathrin ; Drosophila Proteins ; DNM2 protein, Drosophila (EC 3.6.5.5) ; DNM2 protein, mouse (EC 3.6.5.5) ; Dynamin II (EC 3.6.5.5)
    Language English
    Publishing date 2015-10-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108742-0
    ISSN 1460-2083 ; 0964-6906
    ISSN (online) 1460-2083
    ISSN 0964-6906
    DOI 10.1093/hmg/ddv285
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3469: Show issues Location:
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