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J Biol Chem, Vol. 274, Issue 46, 32551-32554, November 12, 1999
§,
, and§
From the § Center for Basic Neuroscience, Secretory
carrier membrane proteins (SCAMPs)
comprise a family of ubiquitous membrane proteins of transport vesicles
with no known function. Their universal presence in all cells suggests a fundamental role in membrane traffic. SCAMPs are particularly highly
expressed in organelles that undergo regulated exocytosis, such as
synaptic vesicles and mast cell granules. Of the three currently known
SCAMPs, SCAMP1 is the most abundant. To investigate the possible
functions of SCAMP1, we generated mice that lack SCAMP1.
SCAMP1-deficient mice are viable and fertile. They exhibit no changes
in the overall architecture or the protein composition of the brain or
alterations in peripheral organs. Capacitance measurements in mast
cells demonstrated that exocytosis could be triggered reliably by
GTP Department of Biochemistry, and
Howard Hughes Medical Institute, University of Texas
Southwestern Medical Center, Dallas, Texas 75235 and ¶ Departmento
de Fisiologia Medica y Biofisica, Facultad de Medicina, Universidad de
Sevilla, Avda. Sanchez-Pizjuan 4, 41009 Sevilla, Spain
S in SCAMP1-deficient cells. The initial overall capacitance of
mast cells was similar between wild type and mutant mice, but the final
cell capacitance after completion of exocytosis, was significantly
smaller in SCAMP1-deficient cells than in wild type cells. Furthermore,
there was an increased proportion of reversible fusion events, which
may have caused the decrease in the overall capacitance change observed
after exocytosis. Our data show that SCAMP1 is not essential for
exocytosis, as such, and does not determine the stability or size of
secretory vesicles, but is required for the full execution of stable
exocytosis in mast cells. This phenotype could be the result of a
function of SCAMP1 in the formation of stable fusion pores during
exocytosis or of a role of SCAMP1 in the regulation of endocytosis
after formation of fusion pores.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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