Regulation and cellular roles of phosphoinositide 5-kinases

Weernink, Paschal A. Oude; Schmidt, Martina; Jakobs, Karl H.

doi:10.1016/j.ejphar.2004.07.014

Cited by 125 publications

(121 citation statements)

References 167 publications

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“…To address these questions, we focused on Phosphatidylinositol Phosphate 5-Kinase (PIP5K), a key enzyme for the production of PtdIns(4,5)P 2 (Oude Weernink et al, 2004). The Arabidopsis genome contains 11 genes encoding proteins with significant sequence similarity to animal PIP5Ks (type I PtdInsP kinases) (Mueller-Roeber and Pical, 2002).…”

Section: Introductionmentioning

confidence: 99%

TheArabidopsisPhosphatidylinositol Phosphate 5-Kinase PIP5K3 Is a Key Regulator of Root Hair Tip Growth

et al. 2008

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Phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P 2 ] functions as a site-specific signal on membranes to promote cytoskeletal reorganization and membrane trafficking. Localization of PtdIns(4,5)P 2 to apices of growing root hairs and pollen tubes suggests that it plays an important role in tip growth. However, its regulation and mode of action remain unclear. We found that Arabidopsis thaliana PIP5K3 (for Phosphatidylinositol Phosphate 5-Kinase 3) encodes a phosphatidylinositol 4-phosphate 5-kinase, a key enzyme producing PtdIns(4,5)P 2 , that is preferentially expressed in growing root hairs. T-DNA insertion mutations that substantially reduced the expression of PIP5K3 caused significantly shorter root hairs than in the wild type. By contrast, overexpression caused longer root hairs and multiple protruding sites on a single trichoblast. A yellow fluorescent protein (YFP) fusion of PIP5K3, driven by the PIP5K3 promoter, complemented the short-root-hair phenotype. PIP5K3-YFP localized to the plasma membrane and cytoplasmic space of elongating root hair apices, to growing root hair bulges, and, notably, to sites about to form root hair bulges. The signal was greatest in rapidly growing root hairs and quickly disappeared when elongation ceased. These results provide evidence that PIP5K3 is involved in localizing PtdIns(4,5)P 2 to the elongating root hair apex and is a key regulator of the machinery that initiates and promotes root hair tip growth.

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Section: Introductionmentioning

confidence: 99%

TheArabidopsisPhosphatidylinositol Phosphate 5-Kinase PIP5K3 Is a Key Regulator of Root Hair Tip Growth

et al. 2008

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“…The major route for PIP 2 synthesis is the phosphorylation of phosphatidylinositol 4-phosphate (PI4P) by type I phosphatidylinositol 4-phosphate 5-kinases (PI4P5-K I) (7)(8)(9). Three PI4P5-K I isoforms (I␣, I␤, and I␥) have been reported, each having alternative splice variants (10,11).…”

Section: P Hosphatidylinositol (4 5)-bisphosphate (Pip 2 )mentioning

confidence: 99%

PI4P5-Kinase Iα Is Required for Efficient HIV-1 Entry and Infection of T Cells

Barrero-Villar

Barroso-González

Cabrero

et al. 2008

The Journal of Immunology

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HIV-1 envelope (Env) triggers membrane fusion between the virus and the target cell. The cellular mechanism underlying this process is not well known. Phosphatidylinositol 4,5-bisphosphate (PIP2) is known to be important for the late steps of the HIV-1 infection cycle by promoting Gag localization to the plasma membrane during viral assembly, but it has not been implicated in early stages of HIV-1 membrane-related events. In this study, we show that binding of the initial HIV-1 Env-gp120 protein induces PIP2 production in permissive lymphocytes through the activation of phosphatidylinositol-4-phosphate 5-kinase (PI4P5-K) Iα. Overexpression of wild-type PI4P5-K Iα increased HIV-1 Env-mediated PIP2 production and enhanced viral replication in primary lymphocytes and CEM T cells, whereas PIP2 production and HIV-1 infection were both severely reduced in cells overexpressing the kinase-dead mutant D227A (D/A)-PI4P5-K Iα. Similar results were obtained with replicative and single-cycle HIV-1 particles. HIV-1 infection was also inhibited by knockdown of endogenous expression of PI4P5-K Iα. These data indicate that PI4P5-K Iα-mediated PIP2 production is crucial for HIV-1 entry and the early steps of infection in permissive lymphocytes.

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“…Phosphorylation of the PIP5Ks is an important mechanism of control for PI(4,5)P2-dependent pathways [Park et al, 2001;Ling et al, 2002;Doughman et al, 2003a;Oude Weernink et al, 2004]. Association with G-proteins also regulates the PIP5K activity.…”

mentioning

confidence: 99%

Phosphatidic acid regulates the affinity of the murine phosphatidylinositol 4‐phosphate 5‐kinase‐Iβ for phosphatidylinositol‐4‐phosphate

Jarquin-Pardo

Fitzpatrick

Galiano

et al. 2006

J of Cellular Biochemistry

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Type I phosphatidylinositol 4-phosphate 5-kinase (PI4P5K) catalyzes the phosphorylation of phosphatidylinositol 4 phosphate [PI(4)P] at carbon 5, producing phosphatidylinositol 4,5 bisphosphate [PI(4,5)P2]. Phosphatidic acid (PA) activates PI4P5K in vitro and plays a central role in the activation of PIP5K pathways in vivo. This report demonstrates that actin fiber formation in murine fibroblasts involves PA activation of PIP5Ks and defines biochemical interactions between PA and the PIP5Ks. Inhibition of phospholipase D production of PA results in the loss of actin fibers. Overexpression of the beta isoform of the type I murine phosphatidylinositol 4-phosphate 5-kinase (mPIP5K-Ib) maintains actin fiber structure in the face of phospholipase D inhibition. PA activates mPIP5K-Ib by direct binding to mPIP5K-Ib through both electrostatic and hydrophobic interactions, with the fatty acid acyl chain length and degree of saturation acting as critical determinants of binding and activation. Furthermore, kinetic analysis suggests that phosphorylation of the PI(4)P substrate does not follow classical Michaelis-Menten kinetics. Instead, the kinetic data are consistent with a model in which mPIP5K-Ib initially binds to the lipid micelle and subsequently binds the PI(4)P substrate. In addition, the kinetics indicate substrate inhibition, suggesting that mPIP5K-Ib contains an inhibitory PI(4)P-binding site. These results suggest a model in which mPIP5K-Ib is surrounded by PI(4)P, but is unable to catalyze its conversion to PI(4,5)P2 unless PA is bound.

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Regulation and cellular roles of phosphoinositide 5-kinases

Cited by 125 publications

References 167 publications

TheArabidopsisPhosphatidylinositol Phosphate 5-Kinase PIP5K3 Is a Key Regulator of Root Hair Tip Growth

TheArabidopsisPhosphatidylinositol Phosphate 5-Kinase PIP5K3 Is a Key Regulator of Root Hair Tip Growth

PI4P5-Kinase Iα Is Required for Efficient HIV-1 Entry and Infection of T Cells

Phosphatidic acid regulates the affinity of the murine phosphatidylinositol 4‐phosphate 5‐kinase‐Iβ for phosphatidylinositol‐4‐phosphate

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