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Vol. 10, Issue 11, 3979-3990, November 1999
and
Medical Research Council Laboratory for Molecular Cell Biology and
Department of Biochemistry and Molecular Biology, University College
London, London WC1E 6BT, United Kingdom
One pathway in forming synaptic-like microvesicles (SLMV) involves
direct budding from the plasma membrane, requires adaptor protein 2 (AP2) and is brefeldin A (BFA) resistant. A second route leads from the
plasma membrane to an endosomal intermediate from which SLMV bud in a
BFA-sensitive, AP3-dependent manner. Because AP3 has been shown to bind
to a di-leucine targeting signal in vitro, we have investigated
whether this major class of targeting signals is capable of directing
protein traffic to SLMV in vivo. We have found that a di-leucine signal
within the cytoplasmic tail of human tyrosinase is responsible for the
majority of the targeting of HRP-tyrosinase chimeras to SLMV in PC12
cells. Furthermore, we have discovered that a Met-Leu di-hydrophobic
motif within the extreme C terminus of synaptotagmin I supports
20% of the SLMV targeting of a CD4-synaptotagmin chimera. All of the
traffic to the SLMV mediated by either di-Leu or Met-Leu is BFA
sensitive, strongly suggesting a role for AP3 and possibly for an
endosomal intermediate in this process. The differential reduction in
SLMV targeting for HRP-tyrosinase and CD4-synaptotagmin chimeras by di-alanine substitutions or BFA treatment implies that different proteins use the two routes to the SLMV to differing extents.
Present address: Cambridge Institute for Medical
Research, Wellcome Trust/Medical Research Council Building,
Addenbrooke's Hospital, Hills Road, Cambridge CB2 2XY, UK.
Corresponding author. E-mail address:
d.cutler{at}ucl.ac.uk.
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