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Vol. 10, Issue 6, 1957-1972, June 1999
*Department of Molecular and Cellular Physiology, Howard Hughes
Medical Institute, Stanford University School of Medicine, Stanford,
California 94305-5345; and The trans-Golgi network (TGN) plays a pivotal role
in directing proteins in the secretory pathway to the appropriate
cellular destination. VAMP4, a recently discovered member of the
vesicle-associated membrane protein (VAMP) family of trafficking
proteins, has been suggested to play a role in mediating TGN
trafficking. To better understand the function of VAMP4, we examined
its precise subcellular distribution. Indirect immunofluorescence and
electron microscopy revealed that the majority of VAMP4 localized to
tubular and vesicular membranes of the TGN, which were in part coated
with clathrin. In these compartments, VAMP4 was found to colocalize
with the putative TGN-trafficking protein syntaxin 6. Additional
labeling was also present on clathrin-coated and noncoated vesicles, on endosomes and the medial and trans side of the Golgi
complex, as well as on immature secretory granules in PC12 cells.
Immunoprecipitation of VAMP4 from rat brain detergent extracts revealed
that VAMP4 exists in a complex containing syntaxin 6. Converging lines
of evidence implicate a role for VAMP4 in TGN-to-endosome transport.
Department of Cell Biology,
School of Medicine, Research Institute for Biomembranes, University of
Utrecht, 3584CX Utrecht, The Netherlands
Corresponding author. E-mail address:
scheller{at}cmgm.stanford.edu.
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