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J Biol Chem, Vol. 275, Issue 2, 1261-1268, January 14, 2000
From the Department of Physiology and Biophysics, University of
Iowa, Iowa City, Iowa 52242
To identify the targeting domains of syntaxin 6 responsible for its localization to the trans-Golgi network
(TGN), we examined the subcellular distribution of enhanced green
fluorescent protein (EGFP) epitope-tagged syntaxin 6/syntaxin 4 chimerae and syntaxin 6 truncation/deletion mutants in 3T3L1
adipocytes. Expression of EGFP-syntaxin 6 resulted in a perinuclear
distribution identical to endogenous syntaxin 6 as determined both by
confocal fluorescence microscopy and subcellular fractionation.
Furthermore, both the endogenous and the expressed EGFP-syntaxin 6 fusion protein were localized to a brefeldin A-insensitive but okadaic
acid-sensitive compartment characteristic of the TGN. In contrast,
EGFP-syntaxin 6 constructs lacking the H2 domain were excluded from the
TGN and were instead primarily localized to the plasma membrane.
Although syntaxin 4 was localized to the plasma membrane, syntaxin
6/syntaxin 4 chimerae and syntaxin 6 truncations containing the H2
domain of syntaxin 6 were predominantly directed to the TGN.
Importantly, the syntaxin 6 H2 domain fused to the transmembrane domain
of syntaxin 4 was also localized to the TGN, demonstrating that the H2
domain was sufficient to confer TGN localization. In addition to the H2
domain, a tyrosine-based plasma membrane internalization signal (YGRL)
was identified between the H1 and H2 domains of syntaxin 6. Deletion of
this sequence resulted in the accumulation of the EGFP-syntaxin 6 reporter construct at the plasma membrane. Together, these data
demonstrate that syntaxin 6 utilizes two distinct domains to drive its
specific subcellular localization to the TGN.
To whom correspondence should be addressed. Tel.: 319-335-7823;
Fax: 319-335-7886; E-mail: jeffrey-pessin@uiowa.edu.
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