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Vol. 13, Issue 6, 1906-1915, June 2002
-Cell Protein Granuphilin Binds Rab3 and Munc-18
and Controls Exocytosis
and
*University of Lausanne, Institut de Biologie Cellulaire et de
Morphologie, Lausanne, Switzerland 1005; and Granuphilin/Slp-4 is a member of the synaptotagmin-like protein
family expressed in pancreatic Ecole
Polytechnique Fédérale, Laboratoire de Neurobiologie
Cellulaire, Lausanne, Switzerland 1005
-cells and in the pituitary gland. We
show by confocal microscopy that both granuphilin-a and -b colocalize
with insulin-containing secretory granules positioned at the periphery
of pancreatic -cells. Overexpression of granuphilins in
insulin-secreting cell lines caused a profound inhibition of stimulus-induced exocytosis. Granuphilins were found to bind to two
components of the secretory machinery of pancreatic -cells, the
small GTP-binding protein Rab3 and the soluble
N-ethylmaleimide-sensitive factor attachment protein
receptor (SNARE)-binding protein Munc-18. The interaction with Rab3
occurred only with the GTP-bound form of the protein and was prevented
by a point mutation in the effector domain of the GTPase.
Structure-function studies using granuphilin-b mutants revealed that
complete loss of Rab3 binding is associated with a reduction in the
capacity to inhibit exocytosis. However, the granuphilin/Rab3 complex
alone is not sufficient to mediate the decrease of exocytosis,
suggesting the existence of additional binding partners. Taken
together, our observations indicate that granuphilins play an important
role in pancreatic -cell exocytosis. In view of the postulated role
of Munc-18 in secretory vesicle docking, our data suggest that
granuphilins may also be involved in this process.
Corresponding author. E-mail:
Romano.Regazzi{at}ibcm.unil.ch.
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