The golgin Lava lamp mediates dynein-based Golgi movements during Drosophila cellularization
- 22 May 2005
- journal article
- letter
- Published by Springer Nature in Nature Cell Biology
- Vol. 7 (6) , 612-618
- https://doi.org/10.1038/ncb1264
Abstract
Drosophila melanogaster cellularization is a dramatic form of cytokinesis in which a membrane furrow simultaneously encapsulates thousands of cortical nuclei of the syncytial embryo to generate a polarized cell layer. Formation of this cleavage furrow depends on Golgi-based secretion and microtubules1,2,3. During cellularization, specific Golgi move along microtubules, first to sites of furrow formation and later to accumulate within the apical cytoplasm of the newly forming cells3. Here we show that Golgi movements and furrow formation depend on cytoplasmic dynein. Furthermore, we demonstrate that Lava lamp (Lva), a golgin protein that is required for cellularization, specifically associates with dynein, dynactin, cytoplasmic linker protein-190 (CLIP-190) and Golgi spectrin, and is required for the dynein-dependent targeting of the secretory machinery. The Lva domains that bind these microtubule-dependent motility factors inhibit Golgi movement and cellularization in a live embryo injection assay. Our results provide new evidence that golgins promote dynein-based motility of Golgi membranes.Keywords
This publication has 29 references indexed in Scilit:
- DYNACTINAnnual Review of Cell and Developmental Biology, 2004
- Reassessing the Role and Dynamics of Nonmuscle Myosin II during Furrow Formation in EarlyDrosophilaEmbryosMolecular Biology of the Cell, 2004
- Dynein: An ancient motor protein involved in multiple modes of transportJournal of Neurobiology, 2003
- The Molecular Motor Toolbox for Intracellular TransportCell, 2003
- βIII Spectrin Binds to the Arp1 Subunit of DynactinJournal of Biological Chemistry, 2001
- Lava Lamp, a Novel Peripheral Golgi Protein, Is Required for Drosophila melanogaster CellularizationThe Journal of cell biology, 2000
- Cytoplasmic Dynein ATPase Activity Is Regulated by Dynactin-dependent PhosphorylationJournal of Biological Chemistry, 2000
- Polarized Insertion of New Membrane from a Cytoplasmic Reservoir during Cleavage of the Drosophila EmbryoThe Journal of cell biology, 2000
- Dynactin increases the processivity of the cytoplasmic dynein motorNature Cell Biology, 1999
- The role of microtubule-based motor proteins in maintaining the structure and function of the Golgi complexBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1998