ArticleDevelopmental biology2015
Drosophila KASH-domain protein Klarsicht regulates microtubule stability and integrin receptor localization during collective cell migration.
Article in Developmental biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 11 citations in OpenAlex.
- Nuclei on the move: LINC complex-dependent and -independent mechanisms of nuclear migration in development.Nucleus (Austin, Tex.) · 2026Review
- Drosophila embryos allocate lipid droplets to specific lineages to ensure punctual development and redox homeostasis.PLoS genetics · 2023Article
- [Regulatory effects of bio-intensity electric field on microtubule acetylation in human epidermal cell line HaCaT].Zhonghua shao shang yu chuang mian xiu fu za zhi · 2022Article
- Crosstalk between basal extracellular matrix adhesion and building of apical architecture during morphogenesis.Biology open · 2021Review
- The LINC complex is required for endothelial cell adhesion and adaptation to shear stress and cyclic stretch.Molecular biology of the cell · 2021Article
- Ablation of SUN2-containing LINC complexes drives cardiac hypertrophy without interstitial fibrosis.Molecular biology of the cell · 2019Article
- Article
- Signal Transduction across the Nuclear Envelope: Role of the LINC Complex in Bidirectional Signaling.Cells · 2019Review
- Microtubule Motors in Establishment of Epithelial Cell Polarity.Cold Spring Harbor perspectives in biology · 2018Review
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
During collective migration of the Drosophila embryonic salivary gland, cells rearrange to form a tube of a distinct shape and size. Here, we report a novel role for the Drosophila Klarsicht-Anc-Syne Homology (KASH) domain protein Klarsicht (Klar) in the regulation of microtubule (MT) stability and integrin receptor localization during salivary gland migration. In wild-type salivary glands, MTs became progressively stabilized as gland migration progressed. In embryos specifically lacking the KASH domain containing isoforms of Klar, salivary gland cells failed to rearrange and migrate, and these defects were accompanied by decreased MT stability and altered integrin receptor localization. In muscles and photoreceptors, KASH isoforms of Klar work together with Klaroid (Koi), a SUN domain protein, to position nuclei; however, loss of Koi had no effect on salivary gland migration, suggesting that Klar controls gland migration through novel interactors. The disrupted cell rearrangement and integrin localization observed in klar mutants could be mimicked by overexpressing Spastin (Spas), a MT severing protein, in otherwise wild-type salivary glands. In turn, promoting MT stability by reducing spas gene dosage in klar mutant embryos rescued the integrin localization, cell rearrangement and gland migration defects. Klar genetically interacts with the Rho1 small GTPase in salivary gland migration and is required for the subcellular localization of Rho1. We also show that Klar binds tubulin directly in vitro. Our studies provide the first evidence that a KASH-domain protein regulates the MT cytoskeleton and integrin localization during collective cell migration.
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