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J. Biol. Chem., Vol. 278, Issue 16, 14121-14133, April 18, 2003
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From the The endoplasmic reticulum/Golgi SNARE
rbet1 cycles between the endoplasmic reticulum and Golgi and is
essential for cargo transport in the secretory pathway. Although the
quaternary SNARE complex containing rbet1 is known to function in
membrane fusion, the structural role of rbet1 is unclear. Furthermore,
the structural determinants for rbet1 targeting and its cyclical
itinerary have not been investigated. We utilized protein interaction
assays to demonstrate that the rbet1 SNARE motif plays a structural
role similar to the carboxyl-terminal helix of SNAP-25 in the synaptic SNARE complex and demonstrated the importance to SNARE complex assembly
of a conserved salt bridge between rbet1 and sec22b. We also examined
the potential role of the rbet1 SNARE motif and SNARE interactions in
rbet1 localization and dynamics. We found that, in contrast to what has
been observed for syntaxin 5, the rbet1 SNARE motif was essential for
proper targeting. To test whether SNARE interactions were important for
the targeting function of the SNARE motif, we used charge repulsion
mutations at the conserved salt bridge position that rendered rbet1
defective for binary, ternary, and quaternary SNARE interactions. We
found that heteromeric SNARE interactions are not required at any step
in rbet1 targeting or dynamics. Furthermore, the heteromeric state of
the SNARE motif does not influence its interaction with the COPI
coat or efficient recruitment onto transport vesicles. We conclude that
protein targeting is a completely independent function of the rbet1
SNARE motif, which is capable of distinct classes of protein interactions.
The SNARE Motif Contributes to rbet1 Intracellular Targeting and
Dynamics Independently of SNARE Interactions*
,,
Department of Molecular, Cellular, and
Developmental Biology, University of Michigan, Ann Arbor, Michigan
48109 and the § Department of Biology, Haverford College,
Haverford, Pennsylvania 19041
*
This work was supported by National Institutes of Health
Grant GM59378 (to J. C. H.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Molecular, Cellular, and Developmental Biology, University of Michigan, 830 North University Ave., Ann Arbor, MI 48109. Tel.:
734-647-6662; Fax: 734-647-0884; E-mail: jessehay@umich.edu.
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