Phosphoinositol diphosphates: non-enzymic formation in vitro and occurrence in vivo in the cellular slime mold Dictyostelium

Mayr, Georg W.; Radenberg, T.; Thiel, Ulrich; Vogel, Günter; Stephens, Len R.

doi:10.1016/0008-6215(92)85052-2

Cited by 47 publications

(39 citation statements)

References 14 publications

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“…2,3 In the early 1990s, a distinct subclass of inositol polyphosphates containing 'high energy' pyrophosphate groups was identified in slime mould and mammalian cells. [4][5][6] Since then several studies have characterized these inositol pyrophosphates (PP-IPs) and their functions (for Akruti Shah 1,2 , Shubhra Ganguli 1,2 , Jayraj Sen 1,2 and Rashna Bhandari reviews see 2,[7][8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23] ). The major PP-IPs, diphosphoinositol pentakisphosphate, PP-IP 5 (or IP 7 ) and bis-diphosphoinositol tetrakisphosphate, [PP] 2 -IP 4 (or IP 8 ), are derived by the addition of phosphate groups to pre-existing monophosphates on IP 6 (Fig.…”

Section: Introductionmentioning

confidence: 99%

“…2 IP 8 is present at much lower levels in most organisms, ranging from undetectable to approximately 50% of IP 7 levels in budding yeast 24 and some mammalian cell lines. of I(1,4,5)P 3 from PI(4,5)P 2 by phospholipase C (PLC), subsequent phosphorylation of IP 3 to IP 4 and IP 5 by inositol polyphosphate multikinase (IPMK or Ipk2), and the conversion of IP 5 to IP 6 by the IP 5 2-kinase, Ipk1. 26 Inositol pyrophosphates are synthesized by two classes of enzymes, IP 6 kinases and PP-IP 5 kinases.…”

Section: Introductionmentioning

confidence: 99%

“…29 1-IP 7 is the minor IP 7 isoform under normal conditions. 2,32 PP-IP 4 and [PP] 2 -IP 3 are derived from IP 5 by the action of IP 6 kinases and PP-IP 5 kinases. 2,33 Diphosphoinositol polyphosphate phosphohydrolase, or DIPP (Ddp1 in S. cerevisiae) hydrolyzes the pyrophosphate moiety of inositol pyrophosphates, rapidly degrading IP 8 to IP 6 34 ( Fig.…”

Section: Introductionmentioning

confidence: 99%

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Inositol Pyrophosphates: Energetic, Omnipresent and Versatile Signalling Molecules

et al. 2017

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| Inositol pyrophosphates (PP-IPs) are a class of energy-rich signalling molecules found in all eukaryotic cells. These are derivatives of inositol that contain one or more diphosphate (or pyrophosphate) groups in addition to monophosphates. The more abundant and best studied PP-IPs are diphosphoinositol pentakisphosphate (IP 7 ) and bis-diphosphoinositol tetrakisphosphate (IP 8 ). These molecules can influence protein function by two mechanisms: binding and pyrophosphorylation. The former involves the specific interaction of a particular inositol pyrophosphate with a binding site on a protein, while the latter is a unique attribute of inositol pyrophosphates, wherein the β-phosphate moiety is transferred from a PP-IP to a pre-phosphorylated serine residue in a protein to generate pyrophosphoserine. Both these events can result in changes in the target protein's activity, localisation or its interaction with other partners. As a consequence of their ubiquitous presence in all eukaryotic organisms and all cell types examined till date, and their ability to modify protein function, PP-IPs have been found to participate in a wide range of metabolic, developmental, and signalling pathways.This review highlights many of the known functions of PP-IPs in the context of their temporal and spatial distribution in eukaryotic cells. The pathway of synthesis of inositol polyphosphates has been characterized in yeast, slime moulds, plants and animals. The simplest anabolic pathway, characterized in the yeast Saccharomyces cerevisiae (Fig. 1) (Fig. 1). Interestingly, the PPIP5Ks also possess a phosphatase domain which selectively cleaves the 1-position β-phosphate of 1-IP 7 and IP 8 , thus targeting the products of the kinase domain.35, 36 A recent study identified another yeast phosphatase, Siw14, that specifically targets the 5-position β-phosphate of PP-IPs 37 (Fig. 1). As PP-IPs are found in all eukaryotic organisms, they display many conserved and divergent 2, 131 Siw14, an inositol pyrophosphate phosphatase in yeast, preferentially cleaves the C5 β-phosphate on PP-IPs. 37 The yeast enzymes are depicted in purple, and mammalian enzymes are depicted in green and are bracketed. The undetermined inositol pyrophosphate structure is represented with an interrogation mark. Myoinositol contains five equatorial (parallel to the axis) and one axial (perpendicular to the axis) hydroxyl groups. Carbon atoms on the myo-inositol ring are numbered on the structures of PI(4,5)P 2 and IP 6 .

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Inositol Pyrophosphates: Energetic, Omnipresent and Versatile Signalling Molecules

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“…Additionally, PP-InsP 5 has been found to decrease as intracellular Ca 21 increases. As diphosphoinositol phosphates contain energy-rich pyrophosphates, it has been speculated that they might serve as phosphate donors in yet unknown phosphorylation reactions [8,9]. There is some preliminary evidence, that PP-InsP 5 phosphorylates protein targets [7].…”

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Diphospho‐myo‐inositol phosphates during the life cycle of Dictyostelium and Polysphondylium

Laussmann

Pikzack

Thiel

et al. 2000

European Journal of Biochemistry

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The intracellular amounts of diphospho-myo-inositol phosphates and InsP 6 were determined in Dictyostelium discoideum AX2 throughout the life cycle, including exponential growth, starvation, differentiation, sporulation and spore germination. Similar experiments were performed with the closely related species Polysphondylium pallidum under conditions resulting in microcyst formation. A distinct accumulation of these compounds is observed during the early starvation phase of the cell population before the onset of the actual differentiation program. When exponentially growing D. discoideum cells were shifted to starvation conditions, a 25-fold accumulation of 5,6-bis-PP-InsP 4 within 3 h was observed. In P. pallidum, the 5,6-bis-PP-InsP 4 pool rises around 20-fold within 8 h during the formation of microcysts from vegetative cells. Finally, the diphosphoinositol phosphates are deposited in spores or microcysts and are degraded when spores or microcysts germinate at low cell density.Keywords: myo-inositol; diphospho-myo-inositol phosphates; Dictyostelium; Polysphondylium.Cellular slime molds like Dictyostelium and Polysphondylium are ancient amoebae that are able to form multicellular aggregates when their food supply is exhausted. The cells of these aggregates differentiate in spore and stalk cells and finally form fruiting bodies. Alternatively, some species can form microcysts as a resistant stage when exposed to increased osmolarity. Under suitable conditions, spores or microcysts can germinate and release solitary living amoebae [1].Diphosphoinositol phosphates were originally discovered in the Dictyostelium discoideum wild-type strain NC4 [2]. In that study, an inositol phosphate derivative was observed that eluted after InsP 6 from an anion-exchange column. It was tentatively suggested that this compound, called`InsP y ', is a`pyrophosphate form of InsP 6 ' [3]. Meanwhile, InsP y from the genus Dictyostelium has been analyzed by HPLC and NMR and was found to consist of three different diphosphoinositol phosphates, namely 5-PP-InsP 5 , 6-PP-InsP 5 , and 5,6-bis-PP-InsP 4 . 5-PP-InsP 5 and 6-PP-InsP 5 can not be completely separated by anion-exchange HPLC but can be distinguished enzymatically using a kinase that specifically phosphorylates 6-PP-InsP 5 but not 5-PP-InsP 5 in isolated PP-InsP 5 fractions. In the closely related genus Polysphondylium, an additional compound of this type has been detected and identified as 1,5-bis-PP-InsP 4 or its enantiomer 3,5-bis-PP-InsP 4 [4,5].The metabolism of highly phosphorylated inositol phosphates during the development of Dictyostelium has been investigated in a previous study by monitoring the incorporation of [ 3 H]inositol into these compounds [3]. It was found that InsP 6 incorporates [ 3 H]inositol continuously for 8 h after onset of starvation. In contrast, no incorporation into InsP y , which corresponds to the sum of diphosphoinositol phosphates, could be seen during the first 3 h of starvation. After this lag phase, InsP y was linearly labeled by [ 3 H]inosit...

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“…Ca 2; could be bound to protein(s) and polyphosphates or highly phosphorylated sugar molecules. In D. discoideum various inositol phosphates are present whose contents increase during development [42][43][44][45]. Electron beam irradiation caused 'bubbling' of MDGs, a phenomenon characteristic for sugar molecules [28].…”

Section: Discussionmentioning

confidence: 99%

Calcium stores in differentiated Dictyostelium discoideum: prespore cells sequester calcium more efficiently than prestalk cells

et al. 2001

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2;-uptake was higher in pellet fractions of prespore than prestalk amoebae (4.7 vs 3.4 nmol/min mg). Ca 2; -release was greater in supernatant fractions from prestalk than prespore cells (16.5 vs 7.7 nmol/10 8 cells). In summary, prestalk and prespore cells possess qualitatively different, high-capacity stores containing distinct amounts of Ca and probably being involved in regulation of the anterior-posterior [Ca 2; ] igradient.

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Phosphoinositol diphosphates: non-enzymic formation in vitro and occurrence in vivo in the cellular slime mold Dictyostelium

Cited by 47 publications

References 14 publications

Inositol Pyrophosphates: Energetic, Omnipresent and Versatile Signalling Molecules

Inositol Pyrophosphates: Energetic, Omnipresent and Versatile Signalling Molecules

Diphospho‐myo‐inositol phosphates during the life cycle of Dictyostelium and Polysphondylium

Calcium stores in differentiated Dictyostelium discoideum: prespore cells sequester calcium more efficiently than prestalk cells

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