The activation of nuclear phosphoinositide 3‐kinase C2β in all‐<i>trans</i>‐retinoic acid‐differentiated HL‐60 cells

Višnjić, Dora; Crljen, Vladiana; Ćurić, Josip; Batinić, Drago; Volinia, Stefano; Banfíƈ, Hrvoje

doi:10.1016/s0014-5793(02)03357-4

Cited by 36 publications

(29 citation statements)

References 33 publications

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“…The pellet at the bottom of the cushion was considered to be the nuclear fraction. 13,23 Preparation of postnuclear membranes was achieved by centrifugation of supernatant, which remained above the cushion after nuclear fraction was obtained. The supernatant was diluted in STM buffer to give final concentration of 162 mM sucrose and spun at 106 000 g for 90 min at 41C in a Beckman SW 28.1 rotor.…”

Section: Isolation Of Nuclei and Postnuclear Membranesmentioning

confidence: 99%

“…The resultant pellet was considered to contain postnuclear membranes. 13,23 Isolation of cytosolic fraction Cytosolic fraction was prepared by homogenization of the cells in a small volume of STM buffer containing all inhibitors as described above. The homogenates were spun at 106 000 g for 90 min at 41C in a Beckman SW 28.1 rotor.…”

Section: Isolation Of Nuclei and Postnuclear Membranesmentioning

confidence: 99%

“…Although ATRA is known to act primarily through the RAR/RXR nuclear receptors, several studies demonstrated the activation of enzymes related to the phosphoinositide signaling pathway in the nuclei of ATRA-differentiated HL-60 cells. 12,13 Class I PI3K activity responsible for the production of PtdIns(3,4,5)P 3 was detected to be bound to nuclear matrices during the ATRAinduced granulocytic differentiation, 14 the ATRA-induced activation of nuclear class I enzymes was mediated by interaction of p85 and Vav adapter, 15 and the granulocytic differentiation was inhibited by either wortmannin or the antisense fragment of p85a. 16 Although the presence of PKC-z in nuclei of ATRAdifferentiated HL-60 cells has been described, 17 the putative activation of other PI3K-downstream targets in nuclei of differentiated cells, including Akt/PKB, has not been investigated.…”

Section: Introductionmentioning

confidence: 99%

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The role of the nuclear Akt activation and Akt inhibitors in all-trans-retinoic acid-differentiated HL-60 cells

et al. 2006

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Section: Isolation Of Nuclei and Postnuclear Membranesmentioning

confidence: 99%

Section: Isolation Of Nuclei and Postnuclear Membranesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The role of the nuclear Akt activation and Akt inhibitors in all-trans-retinoic acid-differentiated HL-60 cells

et al. 2006

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“…Again, the subnuclear localization of PI3K-C2β depends on the cell type. In models of ATRA-differentiated and aphidicolin-synchronized HL-60 cells, the majority of PI3K-C2β activity was detected in the nuclear envelopes (73,74). In contrast to the subnuclear localization, the mechanism of the nuclear PI3K-C2β activation does seem to depend more on the physiological function of the enzyme.…”

Section: Nuclear Class II Phosphoinositide 3-kinasesmentioning

confidence: 87%

“…In contrast, the nuclei of HL-60 cells that were induced to differentiate in the presence of ATRA show a different mechanism of PI3K-C2β activation. Instead of calpain-mediated proteolysis, the activation of PI3K-C2β during differentiation process relies on the tyrosine phosphorylation of the enzyme (73).…”

Section: Nuclear Class II Phosphoinositide 3-kinasesmentioning

confidence: 99%

Nuclear phospholipid signaling: phosphatidylinositol-specific phospholipase C and phosphoinositide 3-kinase

Višnjić

Banfíƈ

2007

Pflugers Arch - Eur J Physiol

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Over the last 20 years, numerous studies have demonstrated the existence of nuclear phosphoinositide signaling distinct from the one at the plasma membrane. The activation of phosphatidylinositol-specific phospholipase C (PI-PLC) and phosphoinositide 3-kinase (PI3K), the generation of diacylglycerol (DAG) and the accumulation of the 3-phosphorylated phosphoinositides have been documented in the nuclei of different cell types.In this review, we summarize some recent studies of the subnuclear localization, mechanisms of activation and the possible physiological roles of the nuclear PI-PLC and PI-3 kinases in the regulation of cell cycle, survival and differentiation.

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The N‐terminus of phosphoinositide 3‐kinase‐C2β regulates lipid kinase activity and binding to clathrin

Wheeler

Domin

2005

Journal Cellular Physiology

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The class II phosphoinositide 3-kinase (PI3K)-C2beta is recruited to polypeptide growth factor receptors following ligand stimulation. In contrast to the class I A p85/p110 heterodimers, this interaction is dependent upon proline residues present within the N-terminal sequence of the 3-phosphoinositide kinase. However, the mechanism by which PI3K-C2beta catalytic activity is regulated currently remains unknown. In many tumours, increased expression of ErbB receptors confers a poor prognosis. We demonstrate that increased expression of EGFR enhanced its association with PI3K-C2beta following stimulation with EGF. Deletion of the first proline rich region within the N-terminus precluded recruitment of PI3K-C2beta to activated EGFR. Although deletion of the first proline rich motif also rendered the enzyme catalytically inactive, further deletions (residues 1-148 and 1-261) that removed the second and third proline rich motifs increased kinase activity. These data confirm a regulatory role for the N-terminus of class II PI3K enzymes suggesting that catalytic activity is regulated by factors that associate with this region during recruitment to activated growth factor receptors. Using an N-terminal PI3K-C2beta-GST fusion protein, clathrin heavy chain was affinity purified from A431 cell lysates. Association of PI3K-C2beta with clathrin was confirmed by co-immunoprecipitation from cell lysates while intracellular co-localisation of PI3K-C2beta and clathrin was confirmed by confocal microscopy. Our findings demonstrate for the first time that the PI3K-C2beta isoform associates with clathrin and thus provides a link between receptor mediated intracellular signalling and clathrin coated vesicle transport.

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The activation of nuclear phosphoinositide 3‐kinase C2β in all‐trans‐retinoic acid‐differentiated HL‐60 cells

Cited by 36 publications

References 33 publications

The role of the nuclear Akt activation and Akt inhibitors in all-trans-retinoic acid-differentiated HL-60 cells

The role of the nuclear Akt activation and Akt inhibitors in all-trans-retinoic acid-differentiated HL-60 cells

Nuclear phospholipid signaling: phosphatidylinositol-specific phospholipase C and phosphoinositide 3-kinase

The N‐terminus of phosphoinositide 3‐kinase‐C2β regulates lipid kinase activity and binding to clathrin

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