Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase

CRAXTON, Andrew; CAFFREY, J. James; BURKHART, William; SAFRANY, T. Stephen; SHEARS, B. Stephen

doi:10.1042/bj3280075

Cited by 82Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesPhytase and its Applications

Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase

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CRAXTON, Andrew, CAFFREY, J. James, BURKHART, William, SAFRANY, T. Stephen, SHEARS, B. Stephen·1997·Biochemical Journal

DOI 10.1042/bj3280075PMC PMC1218889

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Abstract

The characterization of the multiple inositol polyphosphate phosphatase (MIPP) is fundamental to our understanding of how cells control the signalling activities of ‘higher’ inositol polyphosphates. We now describe our isolation of a 2.3 kb cDNA clone of a rat hepatic form of MIPP. The predicted amino acid sequence of MIPP includes an 18 amino acid region that aligned with approximately 60% identity with the catalytic domain of a fungal inositol hexakisphosphate phosphatase (phytase A); the similarity encompassed conservation of the RHGXRXP signature of the histidine acid phosphatase family. A histidine-tagged, truncated form of MIPP was expressed in Escherichia coli and the enzymic specificity of the recombinant protein was characterized: Ins(1,3,4,5,6)P5 was hydrolysed, first to Ins(1,4,5,6)P4 and then to Ins(1,4,5)P3, by consecutive 3- and 6-phosphatase activities. Inositol hexakisphosphate was catabolized without specificity towards a particular phosphate group, but in contrast, MIPP only removed the β-phosphate from the 5-diphosphate group of diphosphoinositol pentakisphosphate. These data, which are consistent with the substrate specificities of native (but not homogeneous) MIPP isolated from rat liver, provide the first demonstration that a single enzyme is responsible for this diverse range of specific catalytic activities. A 2.5 kb transcript of MIPP mRNA was present in all rat tissues that were examined, but was most highly expressed in kidney and liver. The predicted C-terminus of MIPP is comprised of the tetrapeptide SDEL, which is considered a signal for retaining soluble proteins in the lumen of the endoplasmic reticulum; the presence of this sequence provides a molecular explanation for our earlier biochemical demonstration that the endoplasmic reticulum contains substantial MIPP activity [Ali, Craxton and Shears (1993) J. Biol. Chem. 268, 6161-6167].

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The most likely enzyme to generate Ins(1,4,5,6)P4 is PTEN, a well-known tumour suppressor gene that is active in the nucleus and plays a role in chromosome stability.
“The most likely enzyme is the well-known tumour suppressor gene PTEN42,43, which is known to be active in the nucleus and to play a role in chromosome stability (reviewed in44).”
From Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate (2012) · cites this paper as [42]
The ‘Enzymic activity of recombinant MIPP’ section reports that MIPP converts Ins(1,3,4,5,6)P5 to a product consistent with Ins(1,4,5,6)P4. The Discussion identifies MIPP as an endoplasmic-reticulum protein, not nuclear PTEN. The paper does not make the attributed claim about PTEN or chromosome stability. (LLM, conf=0.86)
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Authors: CRAXTON, A., CAFFREY, J. J., BURKHART, W., SAFRANY, T. S., & SHEARS, B. S.
Affiliations: National Institute of Environmental Health Sciences (US)
Glaxo-Wellcome Research and Development, Department of Analytical Chemistry, Research Triangle Park, NC 27709, U.S.A.
Inositide Signaling Section, Laboratory of Signal Transduction, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709, U.S.A.
Corresponding author: CRAXTON, Andrew
ORCID: CRAXTON, Andrew
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1997-11-15
Volume: 328
Issue: 1
Pages: 75-81
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj3280075
PMC: PMC1218889
OpenAlex: W1783261331
Cited by: 82
References: 31
Citations by year: 2026: 2 · 2025: 2 · 2023: 3 · 2022: 3 · 2021: 1 · 2020: 3 · 2019: 1 · 2018: 2 · 2016: 2 · 2015: 3 · 2014: 2 · 2013: 2 · 2012: 4
FWCI: 1.54
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Agricultural and Biological Sciences › Plant Science › Phytase and its Applications
Keywords: inositol polyphosphates, phytic acid, inositol pentakisphosphate, inositol tetrakisphosphate, cDNA cloning, recombinant enzyme expression, tissue expression, endoplasmic reticulum retention, rat liver
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Liver, Molecular Sequence Data, Organ Specificity, Phosphoric Monoester Hydrolases, Recombinant Proteins, RNA, Messenger, DNA, Complementary, Rats

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Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase

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