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6 results on '"Nesprin"'

1. Putting organelles in their place

Author

Patricia Ulm and Verena Jantsch

Subjects
LINC complexes, nuclear envelope, nesprin, nuclear positioning, ER, cellular organisation, Medicine, Science, Biology (General), QH301-705.5
Abstract

Experiments in C. elegans reveal new insights into how the ANC-1 protein helps to anchor the nucleus and other organelles in place.

Published
2021
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2. The Nesprin-1/-2 ortholog ANC-1 regulates organelle positioning in C. elegans independently from its KASH or actin-binding domains

Author

Hongyan Hao, Shilpi Kalra, Laura E Jameson, Leslie A Guerrero, Natalie E Cain, Jessica Bolivar, and Daniel A Starr

Subjects
LINC complexes, nuclear envelope, nesprin, nuclear positioning, ER, Medicine, Science, Biology (General), QH301-705.5
Abstract

KASH proteins in the outer nuclear membrane comprise the cytoplasmic half of linker of nucleoskeleton and cytoskeleton (LINC) complexes that connect nuclei to the cytoskeleton. Caenorhabditis elegans ANC-1, an ortholog of Nesprin-1/2, contains actin-binding and KASH domains at opposite ends of a long spectrin-like region. Deletion of either the KASH or calponin homology (CH) domains does not completely disrupt nuclear positioning, suggesting neither KASH nor CH domains are essential. Deletions in the spectrin-like region of ANC-1 led to significant defects, but only recapitulated the null phenotype in combination with mutations in the transmembrane (TM) span. In anc-1 mutants, the endoplasmic reticulum ER, mitochondria, and lipid droplets were unanchored, moving throughout the cytoplasm. The data presented here support a cytoplasmic integrity model where ANC-1 localizes to the ER membrane and extends into the cytoplasm to position nuclei, ER, mitochondria, and other organelles in place.

Published
2021
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3. The Nesprin-1/-2 ortholog ANC-1 regulates organelle positioning in C. elegans independently from its KASH or actin-binding domains

Author

Shilpi Kalra, Daniel A. Starr, Leslie A Guerrero, Natalie E. Cain, Hongyan Hao, Laura E Jameson, and Jessica Bolivar

Subjects
QH301-705.5, Movement, nuclear positioning, Science, Genetically Modified, Cell Cycle Proteins, Endoplasmic Reticulum, General Biochemistry, Genetics and Molecular Biology, KASH domains, cell biology, Organelle, Genetics, Animals, Protein Interaction Domains and Motifs, Biology (General), Caenorhabditis elegans, Caenorhabditis elegans Proteins, Cytoskeleton, Actin, Cell Nucleus, Organelles, General Immunology and Microbiology, Nesprin, Chemistry, General Neuroscience, Endoplasmic reticulum, Microfilament Proteins, Calcium-Binding Proteins, Nuclear Proteins, LINC complexes, Lipid Droplets, General Medicine, nuclear envelope, Actins, Transmembrane protein, Mitochondria, Cell biology, ER, Cytoplasm, C. elegans, nesprin, Medicine, Generic health relevance, Biochemistry and Cell Biology, Signal Transduction, Protein Binding
Abstract

KASH proteins in the outer nuclear membrane comprise the cytoplasmic half of linker of nucleoskeleton and cytoskeleton (LINC) complexes that connect nuclei to the cytoskeleton. Caenorhabditis elegans ANC-1, an ortholog of Nesprin-1/2, contains actin-binding and KASH domains at opposite ends of a long spectrin-like region. Deletion of either the KASH or calponin homology (CH) domains does not completely disrupt nuclear positioning, suggesting neither KASH nor CH domains are essential. Deletions in the spectrin-like region of ANC-1 led to significant defects, but only recapitulated the null phenotype in combination with mutations in the transmembrane (TM) span. In anc-1 mutants, the endoplasmic reticulum ER, mitochondria, and lipid droplets were unanchored, moving throughout the cytoplasm. The data presented here support a cytoplasmic integrity model where ANC-1 localizes to the ER membrane and extends into the cytoplasm to position nuclei, ER, mitochondria, and other organelles in place.

Published
2021

4. The Nesprin-1/-2 ortholog ANC-1 regulates organelle positioning in

Author

Hongyan, Hao, Shilpi, Kalra, Laura E, Jameson, Leslie A, Guerrero, Natalie E, Cain, Jessica, Bolivar, and Daniel A, Starr

Subjects
Movement, nuclear positioning, Cell Cycle Proteins, Endoplasmic Reticulum, Animals, Genetically Modified, hemic and lymphatic diseases, Animals, Protein Interaction Domains and Motifs, Caenorhabditis elegans, Caenorhabditis elegans Proteins, reproductive and urinary physiology, Cell Nucleus, Organelles, Cellular Organisation, Calcium-Binding Proteins, Microfilament Proteins, Nuclear Proteins, LINC complexes, Lipid Droplets, Cell Biology, nuclear envelope, female genital diseases and pregnancy complications, Actins, Mitochondria, ER, C. elegans, nesprin, Insight, Protein Binding, Signal Transduction
Abstract

KASH proteins in the outer nuclear membrane comprise the cytoplasmic half of linker of nucleoskeleton and cytoskeleton (LINC) complexes that connect nuclei to the cytoskeleton.

Published
2020

5. Putting organelles in their place.

Author

Ulm P and Jantsch V

Subjects
Animals, Cell Nucleus, Caenorhabditis elegans genetics, Nuclear Proteins
Abstract

Experiments in C. elegans reveal new insights into how the ANC-1 protein helps to anchor the nucleus and other organelles in place., Competing Interests: PU, VJ No competing interests declared, (© 2021, Ulm and Jantsch.)

Published
2021
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6. The Nesprin-1/-2 ortholog ANC-1 regulates organelle positioning in C. elegans independently from its KASH or actin-binding domains.

Author

Hao H, Kalra S, Jameson LE, Guerrero LA, Cain NE, Bolivar J, and Starr DA

Subjects
Animals, Animals, Genetically Modified, Caenorhabditis elegans genetics, Caenorhabditis elegans Proteins genetics, Calcium-Binding Proteins metabolism, Cell Nucleus genetics, Cell Nucleus metabolism, Endoplasmic Reticulum genetics, Endoplasmic Reticulum metabolism, Lipid Droplets metabolism, Microfilament Proteins genetics, Mitochondria genetics, Mitochondria metabolism, Movement, Organelles genetics, Protein Binding, Protein Interaction Domains and Motifs, Signal Transduction, Calponins, Actins metabolism, Caenorhabditis elegans metabolism, Caenorhabditis elegans Proteins metabolism, Cell Cycle Proteins metabolism, Microfilament Proteins metabolism, Nuclear Proteins metabolism, Organelles metabolism
Abstract

KASH proteins in the outer nuclear membrane comprise the cytoplasmic half of linker of nucleoskeleton and cytoskeleton (LINC) complexes that connect nuclei to the cytoskeleton. Caenorhabditis elegans ANC-1, an ortholog of Nesprin-1/2, contains actin-binding and KASH domains at opposite ends of a long spectrin-like region. Deletion of either the KASH or calponin homology (CH) domains does not completely disrupt nuclear positioning, suggesting neither KASH nor CH domains are essential. Deletions in the spectrin-like region of ANC-1 led to significant defects, but only recapitulated the null phenotype in combination with mutations in the transmembrane (TM) span. In anc-1 mutants, the endoplasmic reticulum ER, mitochondria, and lipid droplets were unanchored, moving throughout the cytoplasm. The data presented here support a cytoplasmic integrity model where ANC-1 localizes to the ER membrane and extends into the cytoplasm to position nuclei, ER, mitochondria, and other organelles in place., Competing Interests: HH, SK, LJ, LG, NC, JB, DS No competing interests declared, (© 2021, Hao et al.)

Published
2021
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