Effects of mutant lamins on nucleo-cytoskeletal coupling in Drosophila models of LMNA muscular dystrophy

The nuclei of multinucleated skeletal muscles experience substantial external force during development and muscle contraction. Protection from such forces is partly provided by lamins, intermediate filaments that form a scaffold lining the inner nuclear membrane. Lamins play a myriad of roles, inclu...

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Published inFrontiers in cell and developmental biology Vol. 10; p. 934586
Main Authors Shaw, Nicholas M, Rios-Monterrosa, Jose L, Fedorchak, Gregory R, Ketterer, Margaret R, Coombs, Gary S, Lammerding, Jan, Wallrath, Lori L
Format Journal Article
LanguageEnglish
Published Switzerland Frontiers Media S.A 31.08.2022
Subjects
Cell and Developmental Biology
Drosophila
lamins
LINC complex
microtubules
muscular dystrophies
myonuclei
lamins
Drosophila
muscle
LINC complex
microtubules
muscular dystrophies
myonuclei
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Abstract The nuclei of multinucleated skeletal muscles experience substantial external force during development and muscle contraction. Protection from such forces is partly provided by lamins, intermediate filaments that form a scaffold lining the inner nuclear membrane. Lamins play a myriad of roles, including maintenance of nuclear shape and stability, mediation of nuclear mechanoresponses, and nucleo-cytoskeletal coupling. Herein, we investigate how disease-causing mutant lamins alter myonuclear properties in response to mechanical force. This was accomplished a novel application of a micropipette harpooning assay applied to larval body wall muscles of models of lamin-associated muscular dystrophy. The assay enables the measurement of both nuclear deformability and intracellular force transmission between the cytoskeleton and nuclear interior in intact muscle fibers. Our studies revealed that specific mutant lamins increase nuclear deformability while other mutant lamins cause nucleo-cytoskeletal coupling defects, which were associated with loss of microtubular nuclear caging. We found that microtubule caging of the nucleus depended on Msp300, a KASH domain protein that is a component of the linker of nucleoskeleton and cytoskeleton (LINC) complex. Taken together, these findings identified residues in lamins required for connecting the nucleus to the cytoskeleton and suggest that not all muscle disease-causing mutant lamins produce similar defects in subcellular mechanics.
AbstractList The nuclei of multinucleated skeletal muscles experience substantial external force during development and muscle contraction. Protection from such forces is partly provided by lamins, intermediate filaments that form a scaffold lining the inner nuclear membrane. Lamins play a myriad of roles, including maintenance of nuclear shape and stability, mediation of nuclear mechanoresponses, and nucleo-cytoskeletal coupling. Herein, we investigate how disease-causing mutant lamins alter myonuclear properties in response to mechanical force. This was accomplished via a novel application of a micropipette harpooning assay applied to larval body wall muscles of Drosophila models of lamin-associated muscular dystrophy. The assay enables the measurement of both nuclear deformability and intracellular force transmission between the cytoskeleton and nuclear interior in intact muscle fibers. Our studies revealed that specific mutant lamins increase nuclear deformability while other mutant lamins cause nucleo-cytoskeletal coupling defects, which were associated with loss of microtubular nuclear caging. We found that microtubule caging of the nucleus depended on Msp300, a KASH domain protein that is a component of the linker of nucleoskeleton and cytoskeleton (LINC) complex. Taken together, these findings identified residues in lamins required for connecting the nucleus to the cytoskeleton and suggest that not all muscle disease-causing mutant lamins produce similar defects in subcellular mechanics.
The nuclei of multinucleated skeletal muscles experience substantial external force during development and muscle contraction. Protection from such forces is partly provided by lamins, intermediate filaments that form a scaffold lining the inner nuclear membrane. Lamins play a myriad of roles, including maintenance of nuclear shape and stability, mediation of nuclear mechanoresponses, and nucleo-cytoskeletal coupling. Herein, we investigate how disease-causing mutant lamins alter myonuclear properties in response to mechanical force. This was accomplished a novel application of a micropipette harpooning assay applied to larval body wall muscles of models of lamin-associated muscular dystrophy. The assay enables the measurement of both nuclear deformability and intracellular force transmission between the cytoskeleton and nuclear interior in intact muscle fibers. Our studies revealed that specific mutant lamins increase nuclear deformability while other mutant lamins cause nucleo-cytoskeletal coupling defects, which were associated with loss of microtubular nuclear caging. We found that microtubule caging of the nucleus depended on Msp300, a KASH domain protein that is a component of the linker of nucleoskeleton and cytoskeleton (LINC) complex. Taken together, these findings identified residues in lamins required for connecting the nucleus to the cytoskeleton and suggest that not all muscle disease-causing mutant lamins produce similar defects in subcellular mechanics.
The nuclei of multinucleated skeletal muscles experience substantial external force during development and muscle contraction. Protection from such forces is partly provided by lamins, intermediate filaments that form a scaffold lining the inner nuclear membrane. Lamins play a myriad of roles, including maintenance of nuclear shape and stability, mediation of nuclear mechanoresponses, and nucleo-cytoskeletal coupling. Herein, we investigate how disease-causing mutant lamins alter myonuclear properties in response to mechanical force. This was accomplished via a novel application of a micropipette harpooning assay applied to larval body wall muscles of Drosophila models of lamin-associated muscular dystrophy. The assay enables the measurement of both nuclear deformability and intracellular force transmission between the cytoskeleton and nuclear interior in intact muscle fibers. Our studies revealed that specific mutant lamins increase nuclear deformability while other mutant lamins cause nucleo-cytoskeletal coupling defects, which were associated with loss of microtubular nuclear caging. We found that microtubule caging of the nucleus depended on Msp300, a KASH domain protein that is a component of the linker of nucleoskeleton and cytoskeleton (LINC) complex. Taken together, these findings identified residues in lamins required for connecting the nucleus to the cytoskeleton and suggest that not all muscle disease-causing mutant lamins produce similar defects in subcellular mechanics.
The nuclei of multinucleated skeletal muscles experience substantial external force during development and muscle contraction. Protection from such forces is partly provided by lamins, intermediate filaments that form a scaffold lining the inner nuclear membrane. Lamins play a myriad of roles, including maintenance of nuclear shape and stability, mediation of nuclear mechanoresponses, and nucleo-cytoskeletal coupling. Herein, we investigate how disease-causing mutant lamins alter myonuclear properties in response to mechanical force. This was accomplished via a novel application of a micropipette harpooning assay applied to larval body wall muscles of Drosophila models of lamin-associated muscular dystrophy. The assay enables the measurement of both nuclear deformability and intracellular force transmission between the cytoskeleton and nuclear interior in intact muscle fibers. Our studies revealed that specific mutant lamins increase nuclear deformability while other mutant lamins cause nucleo-cytoskeletal coupling defects, which were associated with loss of microtubular nuclear caging. We found that microtubule caging of the nucleus depended on Msp300, a KASH domain protein that is a component of the linker of nucleoskeleton and cytoskeleton (LINC) complex. Taken together, these findings identified residues in lamins required for connecting the nucleus to the cytoskeleton and suggest that not all muscle disease-causing mutant lamins produce similar defects in subcellular mechanics.The nuclei of multinucleated skeletal muscles experience substantial external force during development and muscle contraction. Protection from such forces is partly provided by lamins, intermediate filaments that form a scaffold lining the inner nuclear membrane. Lamins play a myriad of roles, including maintenance of nuclear shape and stability, mediation of nuclear mechanoresponses, and nucleo-cytoskeletal coupling. Herein, we investigate how disease-causing mutant lamins alter myonuclear properties in response to mechanical force. This was accomplished via a novel application of a micropipette harpooning assay applied to larval body wall muscles of Drosophila models of lamin-associated muscular dystrophy. The assay enables the measurement of both nuclear deformability and intracellular force transmission between the cytoskeleton and nuclear interior in intact muscle fibers. Our studies revealed that specific mutant lamins increase nuclear deformability while other mutant lamins cause nucleo-cytoskeletal coupling defects, which were associated with loss of microtubular nuclear caging. We found that microtubule caging of the nucleus depended on Msp300, a KASH domain protein that is a component of the linker of nucleoskeleton and cytoskeleton (LINC) complex. Taken together, these findings identified residues in lamins required for connecting the nucleus to the cytoskeleton and suggest that not all muscle disease-causing mutant lamins produce similar defects in subcellular mechanics.
Author Fedorchak, Gregory R
Wallrath, Lori L
Ketterer, Margaret R
Rios-Monterrosa, Jose L
Shaw, Nicholas M
Coombs, Gary S
Lammerding, Jan
AuthorAffiliation 3 Biology Department , Waldorf University , Forest City , IA , United States
1 Department of Biochemistry , Carver College of Medicine , University of Iowa , Iowa City , IA , United States
2 The Nancy E. and Peter C. Meinig School of Biomedical Engineering , Weill Institute for Cell and Molecular Biology , Cornell University , Ithaca , NY , United States
AuthorAffiliation_xml – name: 2 The Nancy E. and Peter C. Meinig School of Biomedical Engineering , Weill Institute for Cell and Molecular Biology , Cornell University , Ithaca , NY , United States
– name: 3 Biology Department , Waldorf University , Forest City , IA , United States
– name: 1 Department of Biochemistry , Carver College of Medicine , University of Iowa , Iowa City , IA , United States
Author_xml – sequence: 1
  givenname: Nicholas M
  surname: Shaw
  fullname: Shaw, Nicholas M
  organization: Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA, United States
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  givenname: Jose L
  surname: Rios-Monterrosa
  fullname: Rios-Monterrosa, Jose L
  organization: Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA, United States
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  givenname: Gregory R
  surname: Fedorchak
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  organization: The Nancy E. and Peter C. Meinig School of Biomedical Engineering, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY, United States
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  givenname: Margaret R
  surname: Ketterer
  fullname: Ketterer, Margaret R
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  givenname: Gary S
  surname: Coombs
  fullname: Coombs, Gary S
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  organization: The Nancy E. and Peter C. Meinig School of Biomedical Engineering, Weill Institute for Cell and Molecular Biology, Cornell University, Ithaca, NY, United States
– sequence: 7
  givenname: Lori L
  surname: Wallrath
  fullname: Wallrath, Lori L
  organization: Department of Biochemistry, Carver College of Medicine, University of Iowa, Iowa City, IA, United States
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Copyright Copyright © 2022 Shaw, Rios-Monterrosa, Fedorchak, Ketterer, Coombs, Lammerding and Wallrath.
Copyright © 2022 Shaw, Rios-Monterrosa, Fedorchak, Ketterer, Coombs, Lammerding and Wallrath. 2022 Shaw, Rios-Monterrosa, Fedorchak, Ketterer, Coombs, Lammerding and Wallrath
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Keywords lamins
Drosophila
muscle
LINC complex
microtubules
muscular dystrophies
myonuclei
Language English
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Snippet The nuclei of multinucleated skeletal muscles experience substantial external force during development and muscle contraction. Protection from such forces is...
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SubjectTerms Cell and Developmental Biology
Drosophila
lamins
LINC complex
microtubules
muscular dystrophies
myonuclei
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Title Effects of mutant lamins on nucleo-cytoskeletal coupling in Drosophila models of LMNA muscular dystrophy
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