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A more recent version of this article appeared on October 1, 2003
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Submitted on January 20, 2003
Revised on June 10, 2003
Accepted on June 12, 2003
1 Institut de Biologie Cellulaire et de Morphologie, University of Lausanne, Switzerland
2 Fukuda Initiative Research Unit, RIKEN, Saitama, Japan
3 Division de Biochimie Clinique, University of Geneva, Switzerland
4 Unité de Génétique des Déficits Sensoriels CNRS URA 1968, Institut Pasteur, Paris, France
* Corresponding author. E-mail address: Romano.Regazzi{at}ibcm.unil.ch.
Rab27a is a GTPase associated with insulin-containing secretory
granules of pancreatic 
-cells. Selective reduction of Rab27a
expression by RNA interference did not alter granule distribution and
basal secretion but impaired exocytosis triggered by insulin
secretagogues. Screening for potential effectors of the GTPase revealed
that the Rab27a-binding protein Slac2c/MyRIP is associated with
secretory granules of -cells. Attenuation of Slac2c/MyRIP expression
by RNA interference did not modify basal secretion but severely
impaired hormone release in response to secretagogues. Although
-cells express Myosin-Va, a potential partner of Slac2c/MyRIP, no
functional link between the two proteins could be demonstrated. In
fact, overexpression of the Myosin-Va binding domain of Slac2c/MyRIP
did not affect granule localization and hormone exocytosis. In
contrast, overexpression of the actin-binding domain of Slac2c/MyRIP
led to a potent inhibition of exocytosis without detectable alteration
in granule distribution. This effect was prevented by point mutations
that abolish actin binding. Taken together our data suggest that Rab27a
and Slac2c/MyRIP are part of a complex mediating the interaction of
secretory granules with cortical actin cytoskeleton and participate to
the regulation of the final steps of insulin exocytosis.
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