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Vol. 10, Issue 7, 2407-2423, July 1999
Membrane Biology Laboratory, Institute of Molecular and Cell
Biology, Singapore 117609, Republic of Singapore
Members of the syntaxin protein family participate in the
docking-fusion step of several intracellular vesicular transport events. Tlg1p has been identified as a nonessential protein required for efficient endocytosis as well as the maintenance of normal levels
of trans-Golgi network proteins. In this study we
independently describe Tlg1p as an essential protein required for cell
viability. Depletion of Tlg1p in vivo causes a defect in the transport
of the vacuolar protein carboxypeptidase Y through the early Golgi. Temperature-sensitive (ts) mutants of Tlg1p also accumulate the endoplasmic reticulum/cis-Golgi form of
carboxypeptidase Y at the nonpermissive temperature (38°C) and
exhibit underglycosylation of secreted invertase. Overexpression of
Tlg1p complements the growth defect of vti1-11 at the
nonpermissive temperature, whereas incomplete complementation was
observed with vti1-1, further suggesting a role for
Tlg1p in the Golgi apparatus. Overexpression of Sed5p decreases the
viability of tlg1 ts mutants compared with wild-type cells, suggesting that tlg1 ts mutants are more
susceptible to elevated levels of Sed5p. Tlg1p is able to bind
His6-tagged Sec17p (yeast 
-SNAP) in a dose-dependent
manner and enters into a SNARE complex with Vti1p, Tlg2p, and Vps45p.
Morphological analyses by electron microscopy reveal that cells
depleted of Tlg1p or tlg1 ts mutants incubated at the
restrictive temperature accumulate 40- to 50-nm vesicles and experience
fragmentation of the vacuole.
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