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Vol. 10, Issue 11, 3943-3957, November 1999
and
*Biozentrum of the University of Basel, CH-4056 Basel, Switzerland;
Sterols are major components of the plasma membrane, but their
functions in this membrane are not well understood. We isolated a
mutant defective in the internalization step of endocytosis in a gene
(ERG2) encoding a C-8 sterol isomerase that acts in the
late part of the ergosterol biosynthetic pathway. In the absence of
Erg2p, yeast cells accumulate sterols structurally different from
ergosterol, which is the major sterol in wild-type yeast. To
investigate the structural requirements of ergosterol for endocytosis in more detail, several erg mutants
(erg2Institute of Molecular Agrobiology, The National
University of Singapore, Singapore 117604, Republic of Singapore; and
Institut für Biochemie und Lebensmittelchemie,
Technische Universität, A-8010 Graz, Austria
, erg6, and
erg2erg6) were made. Analysis of
fluid phase and receptor-mediated endocytosis indicates that changes in
the sterol composition lead to a defect in the internalization step.
Vesicle formation and fusion along the secretory pathway were not
strongly affected in the erg mutants. The severity of
the endocytic defect correlates with changes in sterol structure and
with the abundance of specific sterols in the erg
mutants. Desaturation of the B ring of the sterol molecules is
important for the internalization step. A single desaturation at C-8,9
was not sufficient to support internalization at 37°C whereas two
double bonds, either at C-5,6 and C-7,8 or at C-5,6 and C-8,9, allowed internalization.
These authors contributed equally to this work.
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