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Volume 270,
Number 9,
Issue of March 3, 1995 pp. 4612-4618
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Developmental
Induction of Golgi Structure and Function in the Primitive Eukaryote Giardia lamblia
(Received for publication, October 3,
1994; and in revised form, November 10, 1994)
Hugo
D.
Luján
,
Alex
Marotta
,
Michael
R.
Mowatt
,
Noah
Sciaky
,
Jennifer
Lippincott-Schwartz
,
Theodore E.
Nash
A fundamental characteristic of eukaryotic cells is the presence
of membrane-bound compartments and membrane transport pathways in which
the Golgi complex plays a central role in the selective processing,
sorting, and secretion of proteins. The parasitic protozoan Giardia
lamblia belongs to the earliest identified lineage among
eukaryotes and therefore offers unique insight into the progression
from primitive to more complex eukaryotic cells. Here, we report that Giardia trophozoites undergo a developmental induction of
Golgi enzyme activities, which correlates with the appearance of a
morphologically identifiable Golgi complex, as they differentiate to
cysts. Prior to this induction, no morphologically or biochemically
identifiable Golgi complex exists within nonencysting cells.
Remarkably, protein secretion in both nonencysting and encysting
trophozoites is inhibited by brefeldin A, and brefeldin A-sensitive
membrane association of ADP-ribosylation factor and -COP is
observed. These results suggest that the secretory machinery of Giardia resembles that of higher eukaryotes despite the
absence of a Golgi complex in nonencysting trophozoites. These findings
have implications both for defining the minimal machinery for protein
secretion in eukaryotes and for examining the biogenesis of Golgi
structure and function.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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