Coordinated intracellular translocation of phosphoinositide-specific phospholipase C-δ with the cell cycle

Yagisawa, Hitoshi; Okada, Masashi; Naito, Yoko; Sasaki, Koh; Yamaga, Masaki; Fujii, Makoto

doi:10.1016/j.bbalip.2006.02.016

Cited by 28 publications

(14 citation statements)

References 96 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The enzyme accumulates in the nucleus during the G 1 /S 1 boundary (1448,1753) following an increase in nuclear PtdIns(4,5)P 2 levels (1448), and it also regulates cell cycle progression (1449). It is not clear how these nuclear changes contribute to the overall functions of the enzyme.…”

Section: Plc␦1mentioning

confidence: 99%

Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation

Balla

2013

Physiological Reviews

1,393

1,655

View full text Add to dashboard Cite

Phosphoinositides (PIs) make up only a small fraction of cellular phospholipids, yet they control almost all aspects of a cell's life and death. These lipids gained tremendous research interest as plasma membrane signaling molecules when discovered in the 1970s and 1980s. Research in the last 15 years has added a wide range of biological processes regulated by PIs, turning these lipids into one of the most universal signaling entities in eukaryotic cells. PIs control organelle biology by regulating vesicular trafficking, but they also modulate lipid distribution and metabolism via their close relationship with lipid transfer proteins. PIs regulate ion channels, pumps, and transporters and control both endocytic and exocytic processes. The nuclear phosphoinositides have grown from being an epiphenomenon to a research area of its own. As expected from such pleiotropic regulators, derangements of phosphoinositide metabolism are responsible for a number of human diseases ranging from rare genetic disorders to the most common ones such as cancer, obesity, and diabetes. Moreover, it is increasingly evident that a number of infectious agents hijack the PI regulatory systems of host cells for their intracellular movements, replication, and assembly. As a result, PI converting enzymes began to be noticed by pharmaceutical companies as potential therapeutic targets. This review is an attempt to give an overview of this enormous research field focusing on major developments in diverse areas of basic science linked to cellular physiology and disease.

show abstract

Section: Plc␦1mentioning

confidence: 99%

Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation

Balla

2013

Physiological Reviews

1,393

1,655

View full text Add to dashboard Cite

show abstract

“…Furthermore, structurefunction relationships of the PLC-d1 PH domain may be modified by alteration of the nature of the membrane. Since PLC-d1 is reported to shuttle between the plasma membrane and the cytoplasm, and also between the cytoplasm and the nucleus [14,15], variations in lipid composition in the different membranes of the cell [16] might cause location-dependent structure-function variations for PLC-d1. Alteration of the asymmetric distribution of lipids between the inner and outer leaflets of the membrane and a lateral segregation of lipid components in the membrane may also cause fluctuations of the lipid composition in the vicinity of PLC-d1.…”

mentioning

confidence: 99%

Phosphatidylserine induces functional and structural alterations of the membrane‐associated pleckstrin homology domain of phospholipase C‐δ1

et al. 2006

Self Cite

View full text Add to dashboard Cite

A number of processes contributing to important cellular functions such as cellular signal transduction, cytoskeletal organization, and membrane trafficking are known to be localized at membrane surfaces of the plasma membrane and organelles. For instance, extracellular signals are often transmitted from activated receptors to peripheral membrane proteins, such heterotrimeric G-proteins, and subsequently amplified and ⁄ or passed to successors by a number of peripheral membrane proteins located at the membrane surface. Because the interface between the aqueous phase and the hydrophobic interior of the membrane provides a unique molecular environment completely different from the homogeneous solution phase environment [1,2], one would expect induction of unique structurefunction relationships for the peripheral membrane The membrane binding affinity of the pleckstrin homology (PH) domain of phospholipase C (PLC)-d1 was investigated using a vesicle coprecipitation assay and the structure of the membrane-associated PH domain was probed using solid-state 13 C NMR spectroscopy. Twenty per cent phosphatidylserine (PS) in the membrane caused a moderate but significant reduction of the membrane binding affinity of the PH domain despite the predicted electrostatic attraction between the PH domain and the head groups of PS. Solid-state NMR spectra of the PH domain bound to the phosphatidylcholine (PC) ⁄ PS ⁄ phosphatidylinositol 4,5-bisphosphate (PIP 2 ) (75 : 20 : 5) vesicle indicated loss of the interaction between the amphipathic a2-helix of the PH domain and the interface region of the membrane which was previously reported for the PH domain bound to PC ⁄ PIP 2 (95 : 5) vesicles. Characteristic local conformations in the vicinity of Ala88 and Ala112 induced by the hydrophobic interaction between the a2-helix and the membrane interface were lost in the structure of the PH domain at the surface of the PC ⁄ PS ⁄ PIP 2 vesicle, and consequently the structure becomes identical to the solution structure of the PH domain bound to d-myo-inositol 1,4,5-trisphosphate. These local structural changes reduce the membrane binding affinity of the PH domain. The effects of PS on the PH domain were reversed by NaCl and MgCl 2 , suggesting that the effects are caused by electrostatic interaction between the protein and PS. These results generally suggest that the structure and function relationships among PLCs and other peripheral membrane proteins that have similar PH domains would be affected by the local lipid composition of membranes.Abbreviations DD-MAS, single pulse excitation dipolar decoupled-magic angle spinning; GST, glutathione-S-transferase; IP 3 , D-myo-inositol 1,4,5-trisphosphate; PC, phosphatidylcholine; PH domain, pleckstrin homology domain; PIP 2 , phosphatidylinositol

show abstract

“…Among all known PI-PLC isoforms, nucleocytoplasmic shuttling is the best documented for PI-PLC-δ 1 -a member of PI-PLC subfamily delta that is the only one present in all eukaryotes (including Plc1p encoded by PLC1 in yeasts) (79). The accumulation of both endogenous enzyme and GFP-PLC-δ 1 construct was observed in leptomycin B-treated MDCK cells and further sequence analysis revealed a nuclear export signal (NES) and a putative NLS-like signal (58,80).…”

Section: Other Nuclear Phospholipase C Isoformsmentioning

confidence: 99%

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

Višnjić

Banfíƈ

2007

Pflugers Arch - Eur J Physiol

View full text Add to dashboard Cite

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.

show abstract

Coordinated intracellular translocation of phosphoinositide-specific phospholipase C-δ with the cell cycle

Cited by 28 publications

References 96 publications

Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation

Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation

Phosphatidylserine induces functional and structural alterations of the membrane‐associated pleckstrin homology domain of phospholipase C‐δ1

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

Contact Info

Product

Resources

About