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J. Biol. Chem., Vol. 275, Issue 31, 24052-24064, August 4, 2000
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From the Department of Biochemistry and Molecular Biology and
** Department of Anatomy and Cell Biology, Monash University,
Clayton, Victoria 3168, Australia, The inositol-polyphosphate 5-phosphatase enzyme
family removes the 5-position phosphate from both inositol phosphate
and phosphoinositide signaling molecules. We have cloned and
characterized a novel 5-phosphatase, which demonstrates a restricted
substrate specificity and tissue expression. The 3.9-kb cDNA
predicts for a 72-kDa protein with an N-terminal proline rich domain, a
central 5-phosphatase domain, and a C-terminal CAAX motif. The
3.9-kilobase mRNA showed a restricted expression but was abundant
in testis and brain. Antibodies against the sequence detected a 72-kDa
protein in the testis in the detergent-insoluble fraction. Indirect
immunofluorescence of the Tera-1 cell line using anti-peptide
antibodies to the 72-kDa 5-phosphatase demonstrated that the enzyme is
predominantly located to the Golgi. Expression of green fluorescent
protein-tagged 72-kDa 5-phosphatase in COS-7 cells revealed that the
enzyme localized predominantly to the Golgi, mediated by the N-terminal
proline-rich domain, but not the C-terminal CAAX motif. In
vitro, the protein inserted into microsomal membranes on
the cytoplasmic face of the membrane. Immunoprecipitated recombinant
72-kDa 5-phosphatase hydrolyzed phosphatidylinositol
3,4,5-trisphosphate and phosphatidylinositol 3,5-bisphosphate, forming
phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol
3-phosphate, respectively. We propose that the novel 5-phosphatase
hydrolyzes phosphatidylinositol 3,4,5-trisphosphate and
phosphatidylinositol 3,5-bisphosphate on the cytoplasmic
Golgi membrane and thereby may regulate Golgi-vesicular trafficking.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF226683.
Cloning and Characterization of a 72-kDa Inositol-polyphosphate
5-Phosphatase Localized to the Golgi Network*
,
,,
Monash Institute for
Reproduction and Development, Monash Medical Centre, Clayton,
Victoria 3168, Australia, and ¶ Joint Protein Structure
Laboratory, Ludwig Institute for Cancer Research and the Walter and
Eliza Hall Institute of Medical Research,
Parkville, Victoria 3050, Australia
*
This work is supported by grants from the National Health
and Medical Research Council of Australia.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.
Recipient of an Australian Postgraduate Research Award.
§
Recipient of an Anti-Cancer Council of Victoria Postgraduate Fellowship.
To whom correspondence should be addressed: Dept. of
Biochemistry and Molecular Biology, Monash University, Clayton,
Victoria 3168, Australia. Tel.: 61399051245; Fax: 61399054699;
E-mail: christina.mitchell@med.monash.edu.au.
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