Cloning and expression of human brain type I inositol 1,4,5‐trisphosphate 5‐phosphatase High levels of mRNA in cerebellar Purkinje cells

Smedt, Florence De; Verjans, Benoît; Mailleux, Pierre; Erneux, Christophé

doi:10.1016/0014-5793(94)00509-5

Cited by 68 publications

(59 citation statements)

References 15 publications

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“…Group I 5-phosphatases have molecular masses of 32-43 kDa and hydrolyze both Ins(1,4,5)P 3 and Ins(1,3,4,5)P 4 but neither PtdIns(4,5)P 2 nor PtdIns(3,4,5)P 3 . Originally purified from platelet cytosol as type I 5-phosphatase (35,46), cDNAs encoding enzymes with similar characteristics have been cloned from a variety of tissue sources (26,27,47). Immunoprecipitation of 5-phosphatase activity from human platelets with antisera to the bovine brain and human placental isozymes suggest that these type I activities may be the same enzyme (48,49).…”

Section: Discussionmentioning

confidence: 99%

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Signaling Inositol Polyphosphate-5-phosphatase

Jefferson¹,

Auethavekiat²,

Pot³

et al. 1997

Journal of Biological Chemistry

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An inositol polyphosphate-5-phosphatase (SIP-110) that binds the SH3 domains of the adaptor protein GRB2 was produced in Sf9 cells and characterized. SIP-110 binds to GRB2 in vitro with a stoichiometry of 1 mol of GRB2/0.7 mol of SIP-110. GRB2 binding does not affect enzyme activity implying that GRB2 serves mainly to localize SIP-110 within cells. SIP-110 hydrolyses inositol (Ins)(1,3,4,5)P 4 to Ins(1,3,4)P 3 . The enzyme does not hydrolyze Ins(1,4,5)P 3 that is a substrate for previously described 5-phosphatases nor does it hydrolyze phosphatidylinositol (PtdIns)(4,5)P 2 . SIP-110 also hydrolyzed PtdIns(3,4,5)P 3 to PtdIns(3,4)P 2 as did recombinant forms of two other 5-phosphatases designated as inositol polyphosphate-5-phosphatase II, and OCRL (the protein that is mutated in oculocerebrorenal syndrome). The inositol polyphosphate-5-phosphatase enzyme family now is represented by at least 9 distinct genes and includes enzymes that fall into 4 subfamilies based on their activities toward various 5-phosphatase substrates.The phosphatidylinositol signaling pathway serves as the signaling mechanism for various extracellular agonists that stimulate calcium ion mobilization, protein phosphorylation, and cell proliferation (1, 2). In response to receptor stimulation, phospholipase C hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P 2 ) 1 to generate Ins(1,4,5)P 3 and diacylglycerol. Ins(1,4,5)P 3 is further converted to Ins(1,3,4,5)P 4 by the action of a 3-kinase. These two soluble inositol phosphates are involved in calcium ion mobilization, and the latter has recently also been suggested to play a role in regulation of a Ras GAP1 (3). Specific 5-phosphatase enzymes hydrolyze Ins(1,4,5)-P 3 and Ins(1,3,4,5)P 4 by converting them to Ins(1,4)P 2 and Ins(1,3,4)P 3 , respectively. These products are inactive in calcium mobilization (1, 2). The phosphatidylinositols PtdIns-(4,5)P 2 and PtdIns(3,4,5)P 3 also serve signaling functions (4). These lipids may regulate cellular secretion (5, 6) and actin assembly (7-9), and they bind various proteins containing protein tyrosine binding, SH2, and pleckstrin homology domains (10 -12). PtdIns(3,4,5)P 3 is absent or maintained at very low levels in most cells except following stimulation with agonists that activate the PtdIns 3-kinase (13-17). Since PtdIns(3,4,5)P 3 is produced after PtdIns 3-kinase activation and is not a substrate for phospholipase C enzymes, it is suggested to act as a second messenger, possibly by activating a serine/threonine kinase, c-Akt (14,18,19).There are now at least 9 distinct genes for 5-phosphatases or proteins with conserved 5-phosphatase sequences. The most recently identified of these are the 110-kDa SIP-110 (20) and the 133-kDa SHIP or . cDNAs encoding these proteins were cloned from human and mouse cDNA libraries, respectively, based on their ability to associate with the adaptor protein GRB2 (20 -22) or their homology to 5-phosphatases or their ability to form complexes with the immunoreceptorbased tyrosine activation motif of ma...

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Section: Discussionmentioning

confidence: 99%

“…Human 5-phosphatase I was expressed as a 412-amino acid protein (26,27) using the pVL1392 baculoviral expression vector and BaculoGold transfection kit from PharMingen. Human 5-phosphatase II used in these studies was 5PtaseS consisting of amino acids 250 -942 of the predicted amino acid sequence (28).…”

Section: Materials-allmentioning

confidence: 99%

Signaling Inositol Polyphosphate-5-phosphatase

Jefferson¹,

Auethavekiat²,

Pot³

et al. 1997

Journal of Biological Chemistry

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“…Isolation of Human SLIM1 and SLIMMER cDNAs-A human bone marrow cDNA library (1 ϫ 10 6 recombinants) was screened using a synthetic oligonucleotide "GCACCATGGCGGGGAAG" derived from the 5-prime end of the human 43-kDa inositol polyphosphate 5-phosphatase (28). The oligonucleotide was labeled with ␥-32 P using polynucleotide kinase and hybridized at 42°C using standard conditions (29).…”

Section: Methodsmentioning

confidence: 99%

“…cDNAs encoding isoforms of SLIM1 were incidentally isolated during attempts to clone the 43-kDa inositol polyphosphate 5-phosphatase (5-phosphatase) (28,32). An oligonucleotide representing nucleotides 95-111 of the Type I 5-phosphatase (28) (GenBank TM accession number X77567) was used to screen 1 ϫ 10 6 plaques of a gt11 human bone marrow library.…”

Section: Isolation Of Cdna Clones Encoding Isoforms Of Slim1-twomentioning

confidence: 99%

Characterization of Two Isoforms of the Skeletal Muscle LIM Protein 1, SLIM1

Brown¹,

Mcgrath²,

Ooms³

et al. 1999

Journal of Biological Chemistry

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We have cloned and characterized a novel isoform of the skeletal muscle LIM protein 1 (SLIM1), designated SLIMMER. SLIM1 contains an N-terminal single zinc finger followed by four LIM domains. SLIMMER is identical to SLIM1 over the first three LIM domains but contains a novel C-terminal 96 amino acids with three potential bipartite nuclear localization signals, a putative nuclear export sequence, and 27 amino acids identical to the RBP-J binding region of KyoT2, a murine isoform of SLIM1. SLIM1 localized to the cytosol of Sol8 myoblasts and myotubes. SLIMMER was detected in the nucleus of myoblasts and, following differentiation into myotubes, was exclusively cytosolic. Recombinant green fluorescent protein-SLIM1 localized to the cytoplasm and associated with focal adhesions and actin filaments in COS-7 cells, while green fluorescent protein-SLIMMER was predominantly nuclear. SLIMMER truncation mutants revealed that the first nuclear localization signal mediates nuclear localization. The addition of the proposed nuclear export sequence decreased the level of exclusively nuclear expression and increased cytosolic SLIMMER expression in COS-7 cells. The leucine-rich nuclear export signal was required for the export of SLIMMER from the nucleus of myoblasts to the cytoplasm of myotubes. Collectively, these results suggest distinct roles for SLIM1 and SLIMMER in focal adhesions and nuclear-cytoplasmic communication.The LIM domain is a double zinc finger motif that mediates the protein-protein interactions of transcription factors, signaling, and cytoskeleton-associated proteins (1-4). LIM is an acronym of the three transcription factors, Lin-11, Isl-1, and Mec-3, in which the motif was first identified (5). The LIM domain contains 50 -60 amino acids, with the consensus sequence (CX 2 CX 17-19 HX 2 C)X 2 (CX 2 CX 16 -20 CX 2 (H/D/C)). The conserved cysteine and histidine residues form two zinc-binding pockets stabilizing the tertiary structure of the protein (6, 7). Despite their structural resemblance to GATA-1 zinc fingers, there is no evidence that LIM domains bind DNA directly. Instead, an increasing number of studies implicate LIM domains in protein-protein interactions that regulate development, cellular differentiation, and the cytoskeleton (8, 9).It has been proposed that LIM proteins form a scaffold upon which the coordinated assembly of proteins occurs (8,10). No single LIM domain-binding motif has been identified. LIM domains can associate with other LIM domains to form homoor heterodimers (8, 11). In addition, LIM domains also bind tyrosine-containing motifs, PDZ domains, ankyrin repeats, and helix-loop-helix domains in proteins lacking LIM domains including tyrosine and serine/threonine kinases, cytoskeletal proteins, and transcription factors (12)(13)(14)(15)(16).LIM proteins have been demonstrated in both the nucleus and cytoplasm. LIM homeodomain and LMO proteins are nuclear proteins, which regulate transcription by forming complexes with other transcription factors (2, 10). Members of the cysteine-rich...

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“…3 -mediated signalling during Shigella invasion. We used an InsP 3 -5 phosphatase (InsP 3 -5P) expressed from a green fluorescent protein (GFP) polycistronic construct to investigate the implication of InsP 3 -mediated Ca 2 þ signalling in Shigella invasion 25 . As expected, InsP 3 -5P-transfected cells did not elicit whole-cell Ca 2 þ responses in response to relevant agonists or to Shigella challenge, indicating efficient inhibition of InsP 3 -mediated signalling (Fig.…”

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confidence: 99%