GOLPH3 Bridges Phosphatidylinositol-4- Phosphate and Actomyosin to Stretch and Shape the Golgi to Promote Budding
Autor: | Michelle M. Ng, Timo Meerloo, Marilyn G. Farquhar, Patricia A. Wiharto, Greg J. Fuchs, Holly C. Dippold, Seth J. Field, Huilin Zhou, Sun-Kyung Lee, Swetha Madhavarapu, Monica L. Kerr, Suzette Farber-Katz, Kenneth A.A. Galbraith, Ronald Sim, Marshall C. Peterman |
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Rok vydání: | 2009 |
Předmět: |
Phosphatidylinositol 4-phosphate
Golgi Apparatus Myosins Biology Article General Biochemistry Genetics and Molecular Biology symbols.namesake chemistry.chemical_compound Phosphatidylinositol Phosphates Myosin Animals Humans Transport Vesicles Golgi localization Secretory pathway Actin Biochemistry Genetics and Molecular Biology(all) Vesicle Membrane Proteins Golgi apparatus Actins Cell biology chemistry Gene Knockdown Techniques symbols CELLBIO Golgi Phosphoprotein 3 Hydrophobic and Hydrophilic Interactions HeLa Cells |
Zdroj: | Cell. 139(2):337-351 |
ISSN: | 0092-8674 |
DOI: | 10.1016/j.cell.2009.07.052 |
Popis: | SummaryGolgi membranes, from yeast to humans, are uniquely enriched in phosphatidylinositol-4-phosphate (PtdIns(4)P), although the role of this lipid remains poorly understood. Using a proteomic lipid-binding screen, we identify the Golgi protein GOLPH3 (also called GPP34, GMx33, MIDAS, or yeast Vps74p) as a PtdIns(4)P-binding protein that depends on PtdIns(4)P for its Golgi localization. We further show that GOLPH3 binds the unconventional myosin MYO18A, thus connecting the Golgi to F-actin. We demonstrate that this linkage is necessary for normal Golgi trafficking and morphology. The evidence suggests that GOLPH3 binds to PtdIns(4)P-rich trans-Golgi membranes and MYO18A conveying a tensile force required for efficient tubule and vesicle formation. Consequently, this tensile force stretches the Golgi into the extended ribbon observed by fluorescence microscopy and the familiar flattened form observed by electron microscopy. |
Databáze: | OpenAIRE |
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