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J. Biol. Chem., Vol. 276, Issue 10, 7643-7653, March 9, 2001
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From the The budding yeast Saccharomyces
cerevisiae has four inositol polyphosphate 5-phosphatase
(5-phosphatase) genes, INP51, INP52, INP53, and
INP54, all of which hydrolyze phosphatidylinositol (4,5)-bisphosphate. INP54 encodes a protein of 44 kDa which
consists of a 5-phosphatase domain and a C-terminal leucine-rich tail, but lacks the N-terminal SacI domain and proline-rich
region found in the other three yeast 5-phosphatases. We report that
Inp54p belongs to the family of tail-anchored proteins and is localized to the endoplasmic reticulum via a C-terminal hydrophobic tail. The
hydrophobic tail comprises the last 13 amino acids of the protein and
is sufficient to target green fluorescent protein to the endoplasmic
reticulum. Protease protection assays demonstrated that the N terminus
of Inp54p is oriented toward the cytoplasm of the cell, with the C
terminus of the protein also exposed to the cytosol. Null mutation of
INP54 resulted in a 2-fold increase in secretion of a
reporter protein, compared with wild-type yeast or cells deleted for
any of the SacI domain-containing 5-phosphatases. We
propose that Inp54p plays a role in regulating secretion, possibly by
modulating the levels of phosphatidylinositol (4,5)-bisphosphate on the
cytoplasmic surface of the endoplasmic reticulum membrane.
The Yeast Inositol Polyphosphate 5-Phosphatase
Inp54p Localizes to the Endoplasmic Reticulum via a C-terminal
Hydrophobic Anchoring Tail
REGULATION OF SECRETION FROM THE ENDOPLASMIC RETICULUM*
§¶,§,,
,,
Department of Biochemistry and Molecular
Biology, Monash University, Clayton, Victoria 3800, Australia, the
PeterMacCallum Cancer Institute, East Melbourne, Victoria 3002, Australia, and the ** Department of Biochemistry and Molecular Biology,
Melbourne University, Parkville, Victoria 3052, Australia
*
This work was supported in part by Australian Research
Council Grant 9606077.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Monash University,
Dept. of Biochemistry and Molecular Biology, Wellington Road, Clayton
Victoria 3800, Australia. Tel.: 61-3-9905-1245; Fax: 61-3-9905-4699; E-mail: Christina.Mitchell@med.monash.edu.au.
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