Myrip couples the capture of secretory granules by the actin-rich cell cortex and their attachment to the plasma membrane
| Autor: | Tim Zeiske, François Darchen, Patricia Meireles, Sébastien Huet, Nathanael Larochette, Isabelle Fanget, Ouardane Jouannot, Claire Desnos |
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| Přispěvatelé: | Institut de Génétique et Développement de Rennes (IGDR), Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Laboratoire de dynamique membranaire et maladies neurologiques (UMR 8192), Université Paris Descartes - Paris 5 (UPD5)-Centre National de la Recherche Scientifique (CNRS), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Institut de Génétique et Développement de Rennes ( IGDR ), Université de Rennes 1 ( UR1 ), Université de Rennes ( UNIV-RENNES ) -Université de Rennes ( UNIV-RENNES ) -Centre National de la Recherche Scientifique ( CNRS ) -Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Laboratoire de dynamique membranaire et maladies neurologiques ( UMR 8192 ), Centre National de la Recherche Scientifique ( CNRS ) -Université Paris Descartes - Paris 5 ( UPD5 ), De Villemeur, Hervé |
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
MESH : Vesicular Transport Proteins
MESH: Vesicular Transport Proteins MESH: Secretory Vesicles Vesicular Transport Proteins MESH : Actins 0302 clinical medicine Myosin MESH : Secretory Vesicles 0303 health sciences MESH: Exocytosis General Neuroscience MESH : Protein Binding Articles Cell biology Biochemistry Protein Binding MESH: Cell Line Tumor MESH : Cell Membrane Exocyst [SDV.BC]Life Sciences [q-bio]/Cellular Biology Biology MESH: Actins MESH : Exocytosis Exocytosis MESH: Cell Adhesion 03 medical and health sciences stomatognathic system MESH : Enterochromaffin Cells Microtubule Cell Line Tumor Cell cortex Cell Adhesion Enterochromaffin Cells Molecular motor Humans MESH: Protein Binding MESH: Enterochromaffin Cells RAB27 [SDV.BC] Life Sciences [q-bio]/Cellular Biology Actin 030304 developmental biology MESH: Humans MESH : Cell Line Tumor [ SDV.BC ] Life Sciences [q-bio]/Cellular Biology Secretory Vesicles MESH : Humans Cell Membrane Actins MESH : Cell Adhesion 030217 neurology & neurosurgery MESH: Cell Membrane |
| Zdroj: | Journal of Neuroscience Journal of Neuroscience, Society for Neuroscience, 2012, 32 (7), pp.2564-77. ⟨10.1523/JNEUROSCI.2724-11.2012⟩ Journal of Neuroscience, 2012, 32 (7), pp.2564-77. ⟨10.1523/JNEUROSCI.2724-11.2012⟩ Journal of Neuroscience, Society for Neuroscience, 2012, 32 (7), pp.2564-77. 〈10.1523/JNEUROSCI.2724-11.2012〉 |
| ISSN: | 0270-6474 1529-2401 |
| DOI: | 10.1523/JNEUROSCI.2724-11.2012⟩ |
| Popis: | International audience; Exocytosis of secretory granules (SGs) requires their delivery to the actin-rich cell cortex followed by their attachment to the plasma membrane (PM). How these reactions are executed and coordinated is still unclear. Myrip, which is also known as Slac-2c, binds to the SG-associated GTPase Rab27 and is thought to promote the delivery of SGs to the PM by recruiting the molecular motor myosin Va. Myrip also interacts with actin and the exocyst complex, suggesting that it may exert multiple roles in the secretory process. By combining total internal reflection fluorescence microscopy, single-particle tracking, a photoconversion-based assay, and mathematical modeling, we show that, in human enterochromaffin cells, Myrip (1) inhibits a class of SG motion characterized by fast and directed movement, suggesting that it facilitates the dissociation of SGs from microtubules; (2) enhances their motion toward the PM and the probability of SG attachment to the PM; and (3) increases the characteristic time of immobilization at the PM, indicating that it is a component of the molecular machinery that tether SGs to the PM. Remarkably, while the first two effects of Myrip depend on its ability to recruit myosin Va on SGs, the third is myosin Va independent but relies on the C-terminal domain of Myrip. We conclude that Myrip couples the retention of SGs in the cell cortex, their transport to the PM, and their attachment to the PM, and thus promotes secretion. These three steps of the secretory process are thus intimately coordinated. |
| Databáze: | OpenAIRE |
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