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Published 10 November 2003. doi:10.1083/jcb.200302157
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© The Rockefeller University Press, 0021-9525/2003/11/559 $8.00
The Journal of Cell Biology, Volume 163, Number 3, 559-570

Article

Rab27A and its effector MyRIP link secretory granules to F-actin and control their motion towards release sites



Claire Desnos1, Jean-Sébastien Schonn1, Sébastien Huet1, Viet Samuel Tran1, Aziz El-Amraoui2, Graça Raposo3, Isabelle Fanget1, Catherine Chapuis1, Gaël Ménasché4, Geneviève de Saint Basile4, Christine Petit2, Sophie Cribier5, Jean-Pierre Henry1 and François Darchen1

1 Centre National de la Recherche Scientifique (CNRS) UPR 1929, Institut de Biologie Physico-Chimique, 75005 Paris, France
2 CNRS URA 1968, Institut Pasteur, 75724 Paris cedex 15, France
3 UMR 144 Curie/CNRS, Institut Curie, 75248 Paris cedex 05, France
4 Institut National de la Santé et de la Recherche Médicale U429, Hôpital Necker, 75743 Paris cedex 15, France
5 CNRS UMR 7099, Institut de Biologie Physico-Chimique, 75005 Paris, France

Address correspondence to François Darchen, Institut de Biologie Physico-Chimique, CNRS UPR 1929, 13 rue Pierre et Marie Curie, 75005 Paris, France. Tel.: 33-1-58-41-50-85. Fax: 33-1-58-41-50-23. email: Francois.Darchen{at}ibpc.fr

The GTPase Rab27A interacts with myosin-VIIa and myosin-Va via MyRIP or melanophilin and mediates melanosome binding to actin. Here we show that Rab27A and MyRIP are associated with secretory granules (SGs) in adrenal chromaffin cells and PC12 cells. Overexpression of Rab27A, GTPase-deficient Rab27A-Q78L, or MyRIP reduced secretory responses of PC12 cells. Amperometric recordings of single adrenal chromaffin cells revealed that Rab27A-Q78L and MyRIP reduced the sustained component of release. Moreover, these effects on secretion were partly suppressed by the actin-depolymerizing drug latrunculin but strengthened by jasplakinolide, which stabilizes the actin cortex. Finally, MyRIP and Rab27A-Q78L restricted the motion of SGs in the subplasmalemmal region of PC12 cells, as measured by evanescent-wave fluorescence microscopy. In contrast, the Rab27A-binding domain of MyRIP and a MyRIP construct that interacts with myosin-Va but not with actin increased the mobility of SGs. We propose that Rab27A and MyRIP link SGs to F-actin and control their motion toward release sites through the actin cortex.

Key Words: Rab27A; MyRIP; exocytosis; actin; neuroendocrine cell

C. Desnos and J.-S. Schonn contributed equally to this work.

The online version of this article includes supplemental material.

Abbreviations used in this paper: 5-HT, 5-hydroxytryptamine; CTL, cytotoxic T lymphocyte; EW-FM, evanescent wave fluorescence microscopy; hGH, human growth hormone; MSD, mean square displacement; NPY, neuropeptide Y; SERT, serotonin transporter; SG, secretory granule.


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