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J. Biol. Chem., Vol. 276, Issue 25, 22810-22818, June 22, 2001
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From the Department of Physiology and Biophysics, University of
Arkansas for Medical Sciences, Little Rock, Arkansas 72205
The roles of the components of the Sec34p
protein complex in intracellular membrane trafficking, first identified
in the yeast Saccharomyces cerevisiae, have yet to be
characterized in higher eukaryotes. We cloned a human cDNA whose
predicted amino acid sequence showed 41% similarity to yeast Sec34p
with homology throughout the entire coding region. Affinity-purified
antibodies raised against the human SEC34 protein (hSec34p) recognized
a cellular protein of 94 kDa in both soluble and membrane fractions.
Like yeast Sec34p, cytosolic hSec34p migrated with an apparent
molecular mass of 300 kDa on a glycerol velocity gradient,
suggesting that it is part of a protein complex. Immunofluorescence
microscopy localized hSec34p to the Golgi compartment in cells of
all species examined, where it co-localized well with the
cis/medial Golgi marker membrin and partially co-localized
with cis-Golgi network marker p115 and
trans-Golgi marker TGN38. The co-localization with membrin
was maintained at 15 °C and after microtubule depolymerization with
nocodazole. During transport of the tsO45 vesicular stomatitis virus G
protein through the Golgi, there was significant overlap with the
hSec34p compartment. Green fluorescent protein-hSec34 expressed
in HeLa cells was restricted to Golgi cisternae, and its membrane
association was sensitive to brefeldin A treatment. Taken together,
our findings indicate that hSec34p is part of a peripheral membrane
protein complex localized on cis/medial Golgi cisternae
where it may participate in tethering intra-Golgi transport vesicles.
Identification of a Human Orthologue of Sec34p as
a Component of the cis-Golgi Vesicle Tethering
Machinery*
*
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 Physiology
and Biophysics, University of Arkansas for Medical Sciences, 4301 W. Markham, Slot 750, Little Rock, AR 72205. Tel.: 501-603-1170; Fax: 501-296-1469; E-mail: lupashinvladimirv@uams.edu.
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