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Vol. 10, Issue 4, 921-933, April 1999
The Molecular and Cell Biology Department, The University of Texas
at Dallas, Richardson, Texas 75083-0688
We noted previously that certain aminoglycoside antibiotics inhibit
the binding of coatomer to Golgi membranes in vitro. The inhibition is mediated in part by two primary amino groups present at
the 1 and 3 positions of the 2-deoxystreptamine moiety of the antibiotics. These two amines appear to mimic the 
-amino groups present in the two lysine residues of the KKXX motif that is known to
bind coatomer. Here we report the effects of
1,3-cyclohexanebis(methylamine) (CBM) on secretion in vivo, a compound
chosen for study because it contains primary amino groups that resemble
those in 2-deoxystreptamine and it should penetrate lipid bilayers more
readily than antibiotics. CBM inhibited coatomer binding to Golgi
membranes in vitro and in vivo and inhibited secretion by intact cells.
Despite depressed binding of coatomer in vivo, the Golgi complex
retained its characteristic perinuclear location in the presence of CBM
and did not fuse with the endoplasmic reticulum (ER). Transport from
the ER to the Golgi was also not blocked by CBM. These data suggest
that a full complement of coat protein I (COPI) on membranes is
not critical for maintenance of Golgi integrity or for traffic from the
ER to the Golgi but is necessary for transport through the Golgi to the
plasma membrane.
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