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Recent studies on proteins residing in the Golgi complex
revealed that the membrane-spanning domain of these proteins are
largely responsible for their retention in the Golgi complex. We show
here that
Volume 270,
Number 20,
Issue of May 19, pp. 12170-12176, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-1,4-Galactosyltransferase
MEMBRANE-SPANNING DOMAIN-DEPENDENT HOMODIMERIZATION AND ASSOCIATION
WITH 
- AND 
-TUBULINS
-1,4-galactosyltransferase (GT) forms homodimers and
large oligomers in vivo, and the formation of the homodimers
is dependent on cysteine and histidine residues within the
transmembrane domain. Double mutations of these residues, Cys
Ser and His
Leu, abolish
homodimerization and simultaneously reduce the Golgi retention.
Co-immunoprecipitation of GT and various GT chimeras with anti-GT and
anti-reporter molecule antibodies revealed that large aggregates of GT
are associated with
- and -tubulins and also with other
cellular proteins. This association between tubulins and GT suggests a
supportive role of the cytoskeleton in the Golgi retention mechanism.
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