المؤلفون: Tzu Lin, Po-Yuan Pan, Yu-Ting Lai, Kai-Wen Chiang, Hsin-Lun Hsieh, Yi-Ping Wu, Jian-Ming Ke, Myong-Chol Lee, Shih-Sian Liao, Hsueh-Tzu Shih, Chiou-Yang Tang, Shi-Bing Yang, Hsu-Chen Cheng, June-Tai Wu, Yuh-Nung Jan, Hsiu-Hsiang Lee

المصدر: PLoS Genetics, Vol 11, Iss 11, p e1005642 (2015)

مصطلحات موضوعية: Genetics, QH426-470

الوصف: During development, certain Drosophila sensory neurons undergo dendrite pruning that selectively eliminates their dendrites but leaves the axons intact. How these neurons regulate pruning activity in the dendrites remains unknown. Here, we identify a coiled-coil protein Spindle-F (Spn-F) that is required for dendrite pruning in Drosophila sensory neurons. Spn-F acts downstream of IKK-related kinase Ik2 in the same pathway for dendrite pruning. Spn-F exhibits a punctate pattern in larval neurons, whereas these Spn-F puncta become redistributed in pupal neurons, a step that is essential for dendrite pruning. The redistribution of Spn-F from puncta in pupal neurons requires the phosphorylation of Spn-F by Ik2 kinase to decrease Spn-F self-association, and depends on the function of microtubule motor dynein complex. Spn-F is a key component to link Ik2 kinase to dynein motor complex, and the formation of Ik2/Spn-F/dynein complex is critical for Spn-F redistribution and for dendrite pruning. Our findings reveal a novel regulatory mechanism for dendrite pruning achieved by temporal activation of Ik2 kinase and dynein-mediated redistribution of Ik2/Spn-F complex in neurons.

وصف الملف: electronic resource

العلاقة: http://europepmc.org/articles/PMC4634852?pdf=renderTest; https://doaj.org/toc/1553-7390Test; https://doaj.org/toc/1553-7404Test

الوصول الحر: https://doaj.org/article/344adb91182c4431b3e2efac028e93aaTest

المؤلفون: Myong-Chol Lee, Min-Jen Tseng, Ya-Hui Chi, Yu-Cheng Huang, Min-Lang Huang, Zhao-Ying Ding, Ying-Hsuan Wang

المصدر: The Journal of Cell Biology

مصطلحات موضوعية: 0301 basic medicine, Genotype, Nuclear Envelope, LINC complex, Transfection, Article, Cell Line, Animals, Genetically Modified, 03 medical and health sciences, Transduction (genetics), 0302 clinical medicine, Ovarian Follicle, Animals, Drosophila Proteins, Humans, Cytoskeleton, Research Articles, Regulation of gene expression, biology, Gene Expression Regulation, Developmental, Membrane Proteins, Cell Biology, biology.organism_classification, Cell biology, Drosophila melanogaster, Phenotype, 030104 developmental biology, Microscopy, Fluorescence, Cytoplasm, Multiprotein Complexes, Female, Signal transduction, 030217 neurology & neurosurgery, Signal Transduction

الوصف: LINC complexes connect the inner and outer nuclear membrane (ONM) to transduce nucleocytoskeletal force. Ding et al. identify an ONM protein, Kuduk/TMEM258, which modulates the quality of LINC complexes and regulates the nuclear envelope architecture, nuclear positioning, and the development of ovarian follicles.
Linker of nucleoskeleton and cytoskeleton (LINC) complexes spanning the nuclear envelope (NE) contribute to nucleocytoskeletal force transduction. A few NE proteins have been found to regulate the LINC complex. In this study, we identify one, Kuduk (Kud), which can reside at the outer nuclear membrane and is required for the development of Drosophila melanogaster ovarian follicles and NE morphology of myonuclei. Kud associates with LINC complex components in an evolutionarily conserved manner. Loss of Kud increases the level but impairs functioning of the LINC complex. Overexpression of Kud suppresses NE targeting of cytoskeleton-free LINC complexes. Thus, Kud acts as a quality control mechanism for LINC-mediated nucleocytoskeletal connections. Genetic data indicate that Kud also functions independently of the LINC complex. Overexpression of the human orthologue TMEM258 in Drosophila proved functional conservation. These findings expand our understanding of the regulation of LINC complexes and NE architecture.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c7e707fd362ee85737fdfebcf540a2cdTest
https://doi.org/10.1083/jcb.201606043Test

المؤلفون: Hsu-Chen Cheng, Kai-Wen Chiang, Hsin-Lun Hsieh, Chiou-Yang Tang, Yu-Ting Lai, Tzu Lin, June-Tai Wu, Shi-Bing Yang, Shih-Sian Liao, Po-Yuan Pan, Yuh Nung Jan, Yi-Ping Wu, Hsiu-Hsiang Lee, Jian-Ming Ke, Hsueh-Tzu Shih, Myong-Chol Lee

المصدر: PLoS Genetics, Vol 11, Iss 11, p e1005642 (2015)
PLoS Genetics

مصطلحات موضوعية: Cytoplasm, Cancer Research, Sensory Receptor Cells, lcsh:QH426-470, Dynein, Sensory system, Dendrite, Microtubule, Genetics, medicine, Animals, Drosophila Proteins, Phosphorylation, Molecular Biology, Genetics (clinical), Ecology, Evolution, Behavior and Systematics, biology, fungi, I-Kappa-B Kinase, Dyneins, Dendrites, Anatomy, biology.organism_classification, I-kappa B Kinase, Cell biology, lcsh:Genetics, Drosophila melanogaster, medicine.anatomical_structure, nervous system, Drosophila Protein, Research Article

الوصف: During development, certain Drosophila sensory neurons undergo dendrite pruning that selectively eliminates their dendrites but leaves the axons intact. How these neurons regulate pruning activity in the dendrites remains unknown. Here, we identify a coiled-coil protein Spindle-F (Spn-F) that is required for dendrite pruning in Drosophila sensory neurons. Spn-F acts downstream of IKK-related kinase Ik2 in the same pathway for dendrite pruning. Spn-F exhibits a punctate pattern in larval neurons, whereas these Spn-F puncta become redistributed in pupal neurons, a step that is essential for dendrite pruning. The redistribution of Spn-F from puncta in pupal neurons requires the phosphorylation of Spn-F by Ik2 kinase to decrease Spn-F self-association, and depends on the function of microtubule motor dynein complex. Spn-F is a key component to link Ik2 kinase to dynein motor complex, and the formation of Ik2/Spn-F/dynein complex is critical for Spn-F redistribution and for dendrite pruning. Our findings reveal a novel regulatory mechanism for dendrite pruning achieved by temporal activation of Ik2 kinase and dynein-mediated redistribution of Ik2/Spn-F complex in neurons.
Author Summary In Drosophila, the nervous systems undergo extensive neuronal remodeling during metamorphosis, as many larval neurons die and adult neurons are generated while some larval neurons survive and prune their branches. Pruning that removes specific parts of neuronal branches without causing cell death is a self-destruct process, thus requiring precise regulation to prevent undesired damage to the nervous systems. Certain Drosophila sensory neurons that undergo dendrite pruning, specifically eliminating the dendrites but leaving the axons intact, provide us an opportunity to study the mechanism of how pruning activity is regulated in the dendrites. We reasoned that the distinctive microtubule polarity in dendrites and axons might be involved and factors are required to regulate the pruning activity in the dendrites through their interaction with microtubules. Here, we identified Spindle-F that mediates Ik2-dependent pruning activity in the dendrites by linking Ik2 to the microtubule motor dynein complex. We showed that elevation of Ik2 activity during dendrite pruning promotes Ik2/Spindle-F/dynein complex moving along the microtubules. We also showed that the formation and redistribution of Ik2/Spindle-F/dynein complex are essential for dendrite pruning. Our study reveals a connection between the polarized microtubules of dendrites and the pruning activity through Spindle-F for dendrite pruning.

الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::182eed586f78c3dd0bda3f26736ccb44Test
https://doi.org/10.1371/journal.pgen.1005642Test

المؤلفون: Zhao-Ying Ding¹, Ying-Hsuan Wang¹, Yu-Cheng Huang¹, Myong-Chol Lee¹, Min-Jen Tseng¹, Min-Lang Huang¹, Ya-Hui Chi²

المصدر: Journal of Cell Biology. Sep2017, Vol. 216 Issue 9, p2827-2841. 15p.

مصطلحات موضوعية: *NUCLEAR membranes, *NUCLEAR matrix, *DROSOPHILA melanogaster

مستخلص: Linker of nucleoskeleton and cytoskeleton (LINC) complexes spanning the nuclear envelope (NE) contribute to nucleocytoskeletal force transduction. A few NE proteins have been found to regulate the LINC complex. In this study, we identify one, Kuduk (Kud), which can reside at the outer nuclear membrane and is required for the development of Drosophila melanogaster ovarian follicles and NE morphology of myonuclei. Kud associates with LINC complex components in an evolutionarily conserved manner. Loss of Kud increases the level but impairs functioning of the LINC complex. Overexpression of Kud suppresses NE targeting of cytoskeleton-free LINC complexes. Thus, Kud acts as a quality control mechanism for LINC-mediated nucleocytoskeletal connections. Genetic data indicate that Kud also functions independently of the LINC complex. Overexpression of the human orthologue TMEM258 in Drosophila proved functional conservation. These findings expand our understanding of the regulation of LINC complexes and NE architecture. [ABSTRACT FROM AUTHOR]