title: The Caenorhabditis elegans SUN protein UNC-84 interacts with lamin to transfer forces from the cytoplasm to the nucleoskeleton during nuclear migration.
abstract: Nuclear migration is a critical component of many cellular and developmental processes. The nuclear envelope forms a barrier between the cytoplasm, where mechanical forces are generated, and the nucleoskeleton. The LINC complex consists of KASH proteins in the outer nuclear membrane and SUN proteins in the inner nuclear membrane that bridge the nuclear envelope. How forces are transferred from the LINC complex to the nucleoskeleton is poorly understood. The Caenorhabditis elegans lamin, LMN-1, is required for nuclear migration and interacts with the nucleoplasmic domain of the SUN protein UNC-84. This interaction is weakened by the unc-84(P91S) missense mutation. These mutant nuclei have an intermediate nuclear migration defect-live imaging of nuclei or LMN-1::GFP shows that many nuclei migrate normally, others initiate migration before subsequently failing, and others fail to begin migration. At least one other component of the nucleoskeleton, the NET5/Samp1/Ima1 homologue SAMP-1, plays a role in nuclear migration. We propose a nut-and-bolt model to explain how forces are dissipated across the nuclear envelope during nuclear migration. In this model, SUN/KASH bridges serve as bolts through the nuclear envelope, and nucleoskeleton components LMN-1 and SAMP-1 act as both nuts and washers on the inside of the nucleus.
authors: Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95618.
authors: Courtney R
authors: CR
authors: Bone
authors: Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95618.
authors: Erin C
authors: EC
authors: Tapley
authors: European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
authors: Mátyás
authors: M
authors: Gorjánácz
authors: Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95618 dastarr@ucdavis.edu.
authors: Daniel A
authors: DA
authors: Starr
mesh_terms: D000818:Animals; D001696:Biomechanical Phenomena; D017173:Caenorhabditis elegans / Q000166:cytology / Q000378:metabolism*; D029742:Caenorhabditis elegans Proteins / Q000378:metabolism*; D002467:Cell Nucleus / Q000502:physiology*; D003593:Cytoplasm / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism; D007797:Laminin / Q000378:metabolism*; D007814:Larva / Q000166:cytology / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism*; D009687:Nuclear Proteins / Q000378:metabolism*; D054730:Protein Interaction Domains and Motifs; D021381:Protein Transport
chemical_list: D029742:Caenorhabditis elegans Proteins; C570326:LMN-1 protein, C elegans; D007797:Laminin; D008562:Membrane Glycoproteins; D009687:Nuclear Proteins; C120560:Unc-84 protein, C elegans