A mutation associated with centronuclear myopathy enhances the size and stability of dynamin 2 complexes in cells
Dynamin 2 (Dyn2) is a ~100kDa GTPase that assembles around the necks of nascent endocytic and Golgi vesicles and catalyzes membrane scission. Mutations in Dyn2 that cause centronuclear myopathy (CNM) have been shown to stabilize Dyn2 polymers against GTP-dependent disassembly in vitro. Precisely tim...
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| Published in | Biochimica et biophysica acta Vol. 1840; no. 1; pp. 315 - 321 |
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| Main Authors | , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Elsevier B.V
01.01.2014
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| Online Access | Get full text |
| ISSN | 0304-4165 0006-3002 1872-8006 |
| DOI | 10.1016/j.bbagen.2013.09.001 |
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| Abstract | Dynamin 2 (Dyn2) is a ~100kDa GTPase that assembles around the necks of nascent endocytic and Golgi vesicles and catalyzes membrane scission. Mutations in Dyn2 that cause centronuclear myopathy (CNM) have been shown to stabilize Dyn2 polymers against GTP-dependent disassembly in vitro. Precisely timed regulation of assembly and disassembly is believed to be critical for Dyn2 function in membrane vesiculation, and the CNM mutations interfere with this regulation by shifting the equilibrium toward the assembled state.
In this study we use two fluorescence fluctuation spectroscopy (FFS) approaches to show that a CNM mutant form of Dyn2 also has a greater propensity to self-assemble in the cytosol and on the plasma membrane of living cells.
Results obtained using brightness analysis indicate that unassembled wild-type Dyn2 is predominantly tetrameric in the cytosol, although different oligomeric species are observed, depending on the concentration of expressed protein. In contrast, an R369W mutant identified in CNM patients forms higher-order oligomers at concentrations above 1μM. Investigation of Dyn2-R369W by Total Internal Reflection Fluorescence (TIRF) FFS reveals that this mutant forms larger and more stable clathrin-containing structures on the plasma membrane than wild-type Dyn2.
These observations may explain defects in membrane trafficking reported in CNM patient cells and in heterologous systems expressing CNM-associated Dyn2 mutants.
•The properties of a CNM-associated dynamin mutant in living cells are studied using fluorescence.•The R369W dynamin mutant forms larger oligomers in the cytosol than does wild-type dynamin.•The R369W dynamin assembles into large polymers on clathrin-coated pits in the plasma membrane.•These observations provide insight into the molecular defects underlying dynamin-dependent CNM. |
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| AbstractList | Dynamin 2 (Dyn2) is a ~100kDa GTPase that assembles around the necks of nascent endocytic and Golgi vesicles and catalyzes membrane scission. Mutations in Dyn2 that cause centronuclear myopathy (CNM) have been shown to stabilize Dyn2 polymers against GTP-dependent disassembly in vitro. Precisely timed regulation of assembly and disassembly is believed to be critical for Dyn2 function in membrane vesiculation, and the CNM mutations interfere with this regulation by shifting the equilibrium toward the assembled state.In this study we use two fluorescence fluctuation spectroscopy (FFS) approaches to show that a CNM mutant form of Dyn2 also has a greater propensity to self-assemble in the cytosol and on the plasma membrane of living cells.Results obtained using brightness analysis indicate that unassembled wild-type Dyn2 is predominantly tetrameric in the cytosol, although different oligomeric species are observed, depending on the concentration of expressed protein. In contrast, an R369W mutant identified in CNM patients forms higher-order oligomers at concentrations above 1μM. Investigation of Dyn2-R369W by Total Internal Reflection Fluorescence (TIRF) FFS reveals that this mutant forms larger and more stable clathrin-containing structures on the plasma membrane than wild-type Dyn2.These observations may explain defects in membrane trafficking reported in CNM patient cells and in heterologous systems expressing CNM-associated Dyn2 mutants. Dynamin 2 (Dyn2) is a ~100kDa GTPase that assembles around the necks of nascent endocytic and Golgi vesicles and catalyzes membrane scission. Mutations in Dyn2 that cause centronuclear myopathy (CNM) have been shown to stabilize Dyn2 polymers against GTP-dependent disassembly in vitro. Precisely timed regulation of assembly and disassembly is believed to be critical for Dyn2 function in membrane vesiculation, and the CNM mutations interfere with this regulation by shifting the equilibrium toward the assembled state. In this study we use two fluorescence fluctuation spectroscopy (FFS) approaches to show that a CNM mutant form of Dyn2 also has a greater propensity to self-assemble in the cytosol and on the plasma membrane of living cells. Results obtained using brightness analysis indicate that unassembled wild-type Dyn2 is predominantly tetrameric in the cytosol, although different oligomeric species are observed, depending on the concentration of expressed protein. In contrast, an R369W mutant identified in CNM patients forms higher-order oligomers at concentrations above 1μM. Investigation of Dyn2-R369W by Total Internal Reflection Fluorescence (TIRF) FFS reveals that this mutant forms larger and more stable clathrin-containing structures on the plasma membrane than wild-type Dyn2. These observations may explain defects in membrane trafficking reported in CNM patient cells and in heterologous systems expressing CNM-associated Dyn2 mutants. Dynamin 2 (Dyn2) is a ~100kDa GTPase that assembles around the necks of nascent endocytic and Golgi vesicles and catalyzes membrane scission. Mutations in Dyn2 that cause centronuclear myopathy (CNM) have been shown to stabilize Dyn2 polymers against GTP-dependent disassembly in vitro. Precisely timed regulation of assembly and disassembly is believed to be critical for Dyn2 function in membrane vesiculation, and the CNM mutations interfere with this regulation by shifting the equilibrium toward the assembled state. In this study we use two fluorescence fluctuation spectroscopy (FFS) approaches to show that a CNM mutant form of Dyn2 also has a greater propensity to self-assemble in the cytosol and on the plasma membrane of living cells. Results obtained using brightness analysis indicate that unassembled wild-type Dyn2 is predominantly tetrameric in the cytosol, although different oligomeric species are observed, depending on the concentration of expressed protein. In contrast, an R369W mutant identified in CNM patients forms higher-order oligomers at concentrations above 1μM. Investigation of Dyn2-R369W by Total Internal Reflection Fluorescence (TIRF) FFS reveals that this mutant forms larger and more stable clathrin-containing structures on the plasma membrane than wild-type Dyn2. These observations may explain defects in membrane trafficking reported in CNM patient cells and in heterologous systems expressing CNM-associated Dyn2 mutants. •The properties of a CNM-associated dynamin mutant in living cells are studied using fluorescence.•The R369W dynamin mutant forms larger oligomers in the cytosol than does wild-type dynamin.•The R369W dynamin assembles into large polymers on clathrin-coated pits in the plasma membrane.•These observations provide insight into the molecular defects underlying dynamin-dependent CNM. Dynamin 2 (Dyn2) is a ~100kDa GTPase that assembles around the necks of nascent endocytic and Golgi vesicles and catalyzes membrane scission. Mutations in Dyn2 that cause centronuclear myopathy (CNM) have been shown to stabilize Dyn2 polymers against GTP-dependent disassembly in vitro. Precisely timed regulation of assembly and disassembly is believed to be critical for Dyn2 function in membrane vesiculation, and the CNM mutations interfere with this regulation by shifting the equilibrium toward the assembled state.BACKGROUNDDynamin 2 (Dyn2) is a ~100kDa GTPase that assembles around the necks of nascent endocytic and Golgi vesicles and catalyzes membrane scission. Mutations in Dyn2 that cause centronuclear myopathy (CNM) have been shown to stabilize Dyn2 polymers against GTP-dependent disassembly in vitro. Precisely timed regulation of assembly and disassembly is believed to be critical for Dyn2 function in membrane vesiculation, and the CNM mutations interfere with this regulation by shifting the equilibrium toward the assembled state.In this study we use two fluorescence fluctuation spectroscopy (FFS) approaches to show that a CNM mutant form of Dyn2 also has a greater propensity to self-assemble in the cytosol and on the plasma membrane of living cells.METHODSIn this study we use two fluorescence fluctuation spectroscopy (FFS) approaches to show that a CNM mutant form of Dyn2 also has a greater propensity to self-assemble in the cytosol and on the plasma membrane of living cells.Results obtained using brightness analysis indicate that unassembled wild-type Dyn2 is predominantly tetrameric in the cytosol, although different oligomeric species are observed, depending on the concentration of expressed protein. In contrast, an R369W mutant identified in CNM patients forms higher-order oligomers at concentrations above 1μM. Investigation of Dyn2-R369W by Total Internal Reflection Fluorescence (TIRF) FFS reveals that this mutant forms larger and more stable clathrin-containing structures on the plasma membrane than wild-type Dyn2.RESULTSResults obtained using brightness analysis indicate that unassembled wild-type Dyn2 is predominantly tetrameric in the cytosol, although different oligomeric species are observed, depending on the concentration of expressed protein. In contrast, an R369W mutant identified in CNM patients forms higher-order oligomers at concentrations above 1μM. Investigation of Dyn2-R369W by Total Internal Reflection Fluorescence (TIRF) FFS reveals that this mutant forms larger and more stable clathrin-containing structures on the plasma membrane than wild-type Dyn2.These observations may explain defects in membrane trafficking reported in CNM patient cells and in heterologous systems expressing CNM-associated Dyn2 mutants.CONCLUSIONS AND GENERAL SIGNIFICANCEThese observations may explain defects in membrane trafficking reported in CNM patient cells and in heterologous systems expressing CNM-associated Dyn2 mutants. |
| Author | Digman, Michelle A. Li, Jinhui Mueller, Joachim D. Gratton, Enrico Albanesi, Joseph P. Ross, Justin A. Wang, Lei James, Nicholas G. Jameson, David M. Barylko, Barbara Chen, Yan |
| AuthorAffiliation | 2 Laboratory for Fluorescence Dynamics, Department of Biomedical Engineering, University of California, Irvine, California 92697 1 Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii, 651 Ilalo Street, Biosciences 222, Honolulu, Hawaii 96813 3 Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, Texas 75390-9041 4 School of Physics and Astronomy, University of Minnesota, Minneapolis, Minnesota 55455 |
| AuthorAffiliation_xml | – name: 2 Laboratory for Fluorescence Dynamics, Department of Biomedical Engineering, University of California, Irvine, California 92697 – name: 1 Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii, 651 Ilalo Street, Biosciences 222, Honolulu, Hawaii 96813 – name: 3 Department of Pharmacology, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd., Dallas, Texas 75390-9041 – name: 4 School of Physics and Astronomy, University of Minnesota, Minneapolis, Minnesota 55455 |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24016602$$D View this record in MEDLINE/PubMed |
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| Keywords | PSF CNM ACF Fluorescence fluctuation spectroscopy GED R369W N&B EMCCD EGFP TIRF MEF FFS R369W mutation PCH Dyn2-EGFP Dyn PH ICS CME Centronuclear myopathy Dynamin 2 wt PM Mouse embryo fibroblasts rat dynamin 2 isoform 2ba with a C- terminal EGFP and terminal hexa-histidine tag point spread function Number and Brightness autocorrelation function Pleckstrin Homology Image Correlation Spectroscopy Clathrin-mediated endocytosis plasma membrane GTPase effector domain Photon Counting Histogram Total Internal Reflection Fluorescence rat dynamin 2 isoform 2ba construct containing an Arg to Trp mutation at residue 369 electron multiplying charge-coupled device Dynamin wild-type |
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| SubjectTerms | Animals Bone Neoplasms - genetics Bone Neoplasms - metabolism Bone Neoplasms - pathology Cell Membrane - metabolism Cells, Cultured Centronuclear myopathy Clathrin - metabolism cytosol Cytosol - metabolism Dynamin 2 Dynamin II - genetics Dynamin II - metabolism dynamins EGFP Embryo, Mammalian - cytology Embryo, Mammalian - metabolism Endocytosis Fibroblasts - cytology Fibroblasts - metabolism fluorescence Fluorescence fluctuation spectroscopy Golgi Apparatus - metabolism Humans Image Processing, Computer-Assisted Mice Microscopy, Fluorescence muscular diseases mutants mutation Mutation - genetics Myopathies, Structural, Congenital - genetics Myopathies, Structural, Congenital - metabolism Myopathies, Structural, Congenital - pathology Osteosarcoma - genetics Osteosarcoma - metabolism Osteosarcoma - pathology patients physiological transport plasma membrane polymers Protein Multimerization - genetics Protein Transport R369W mutation spectroscopy TIRF |
| Title | A mutation associated with centronuclear myopathy enhances the size and stability of dynamin 2 complexes in cells |
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