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Vol. 10, Issue 12, 4163-4176, December 1999
*Department of Cell Biology, University Medical Centre and
Institute for Biomembranes, Utrecht University, 3584 CX Utrecht, The
Netherlands; and The putative role of sorting early endosomes (EEs) in synaptic-like
microvesicle (SLMV) formation in the neuroendocrine PC12 cell line was
investigated by quantitative immunoelectron microscopy. By BSA-gold
internalization kinetics, four distinct endosomal subcompartments were
distinguished: primary endocytic vesicles, EEs, late endosomes, and
lysosomes. As in other cells, EEs consisted of vacuolar and
tubulovesicular subdomains. The SLMV marker proteins synaptophysin and
vesicle-associated membrane protein 2 (VAMP-2) localized to both
the EE vacuoles and associated tubulovesicles. Quantitative analysis
showed that the transferrin receptor and SLMV proteins colocalized to a
significantly higher degree in primary endocytic vesicles then in
EE-associated tubulovesicles. By incubating PC12 cells expressing T
antigen-tagged VAMP (VAMP-TAg) with antibodies against the luminal TAg,
the recycling pathway of SLMV proteins was directly visualized. At
15°C, internalized VAMP-TAg accumulated in the vacuolar domain of
EEs. Upon rewarming to 37°C, the labeling shifted to the tubular part
of EEs and to newly formed SLMVs. Our data delineate a pathway in which
SLMV proteins together with transferrin receptor are delivered
to EEs, where they are sorted into SLMVs and recycling vesicles, respectively.
Department of Biochemistry and
Biophysics, Hormone Research Institute, University of California, San
Francisco, California 94143-0534
Corresponding author. E-mail
address: J.Klumperman{at}lab.azu.nl.
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