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Vol. 11, Issue 8, 2719-2731, August 2000
and
*Department of Molecular and Cellular Physiology, Howard Hughes
Medical Institute, Stanford University School of Medicine, Stanford,
California 94305-5345; and The endoplasmic reticulum (ER) consists of subcompartments that
have distinct protein constituents, morphological appearances, and
functions. To understand the mechanisms that regulate the intricate and
dynamic organization of the endoplasmic reticulum, it is important to
identify and characterize the molecular machinery involved in the
assembly and maintenance of the different subcompartments. Here we
report that syntaxin 17 is abundantly expressed in steroidogenic cell
types and specifically localizes to smooth membranes of the ER. By
immunoprecipitation analyses, syntaxin 17 exists in complexes with a
syntaxin regulatory protein, rsly1, and/or two intermediate compartment
SNARE proteins, rsec22b and rbet1. Furthermore, we found that syntaxin
17 is anchored to the smooth endoplasmic reticulum through an unusual
mechanism, requiring two adjacent hydrophobic domains near its carboxyl
terminus. Converging lines of evidence indicate that syntaxin 17 functions in a vesicle-trafficking step to the smooth-surfaced tubular
ER membranes that are abundant in steroidogenic cells.
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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