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Vol. 11, Issue 6, 1989-2005, June 2000
and
*Department of Cell Biology and Yeast phosphatidylinositol transfer protein (Sec14p) is
essential for Golgi function and cell viability. We now report a
characterization of five yeast SFH (Sec Fourteen
Homologue) proteins that share 24-65% primary sequence identity with
Sec14p. We show that Sfh1p, which shares 64% primary sequence identity
with Sec14p, is nonfunctional as a Sec14p in vivo or in vitro. Yet,
SFH proteins sharing low primary sequence similarity
with Sec14p (i.e., Sfh2p, Sfh3p, Sfh4p, and Sfh5p) represent novel
phosphatidylinositol transfer proteins (PITPs) that exhibit
phosphatidylinositol- but not phosphatidylcholine-transfer activity in vitro. Moreover, increased expression of Sfh2p, Sfh4p, or
Sfh5p rescues sec14-associated growth and secretory
defects in a phospholipase D (PLD)-sensitive manner. Several
independent lines of evidence further demonstrate that
SFH PITPs are collectively required for efficient
activation of PLD in vegetative cells. These include a collective
requirement for SFH proteins in Sec14p-independent cell
growth and in optimal activation of PLD in Sec14p-deficient cells.
Consistent with these findings, Sfh2p colocalizes with PLD in endosomal
compartments. The data indicate that SFH gene products
cooperate with "bypass-Sec14p" mutations and PLD in a complex
interaction through which yeast can adapt to loss of the essential
function of Sec14p. These findings expand the physiological repertoire
of PITP function in yeast and provide the first in vivo demonstration
of a role for specific PITPs in stimulating activation of PLD.
Department of
Biochemistry and Molecular Genetics, University of Alabama at
Birmingham, Birmingham, Alabama 35294-0005; §Department of
Biology, Indiana University-Purdue University at Indianapolis,
Indianapolis, Indiana 46202-5132; and Wyeth Ayerst
Research, Princeton, New Jersey 08543-8000
These authors contributed equally to this work.
¶
Corresponding author. E-mail address:
vabankaitis{at}bmg.bhs.uab.edu.
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