Generation of phosphatidylinositol 4,5‐bisphosphate proceeds through an intracellular route in rat hepatocytes

Lundberg, Gunilla A.; Jergil, Bengt

doi:10.1016/0014-5793(88)80362-4

Cited by 29 publications

(11 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…We also found PLCδ " PH-GST labelling on the rough endoplasmic reticulum, Golgi structures and endosomes, providing direct in situ evidence for pools of PtdIns(4,5)P # in the secretory and endocytic pathways. Our endoplasmic-reticulum data are consistent with studies showing phosphatidylinositol synthase activity and PtdIns(4,5)P # synthesis [43,44] in microsomal fractions. More specifically, phosphatidylinositol 4-kinase α, as well as a novel phosphatidylinositol-5-phosphate 4-kinase (phosphatidylinositol-phosphate kinase IIγ), has been identified on endoplasmic-reticulum membranes [45,46], and a yeast PtdIns(4,5)P # 5-phosphatase Inp54 located on the endoplasmic reticulum exerts negative control of secretion [47].…”

Section: Discussionsupporting

confidence: 92%

Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C δ1

Watt

Kular

Fleming

et al. 2002

Biochemical Journal

247

View full text Add to dashboard Cite

Ptd(4,5)P2 is thought to promote and organize a wide range of cellular functions, including vesicular membrane traffic and cytoskeletal dynamics, by recruiting functional protein complexes to restricted locations in cellular membranes. However, little is known about the distribution of PtdIns(4,5)P2 in the cell at high resolution. We have used the pleckstrin homology (PH) domain of phospholipase δ1 (PLCδ1), narrowly specific for PtdIns(4,5)P2, to map the distribution of the lipid in astrocytoma and A431 cells. We applied the glutathione S-transferase-tagged PLCδ1 PH domain (PLCδ1PH—GST) in an on-section labelling approach which avoids transfection procedures. Here we demonstrate PtdIns(4,5)P2 labelling in the plasma membrane, and also in intracellular membranes, including Golgi (mainly stack), endosomes and endoplasmic reticulum, as well as in electron-dense structures within the nucleus. At the plasma membrane, labelling was more concentrated over lamellipodia, but not in caveolae, which contained less than 10% of the total cell-surface labelling. A dramatic decrease in signal over labelled compartments was observed on preincubation with the cognate headgroup [Ins(1,4,5)P3], and plasma-membrane labelling was substantially decreased after stimulation with thrombin-receptor-activating peptide (SFLLRN in the one-letter amino acid code), a treatment which markedly diminishes PtdIns(4,5)P2 levels. Thus we have developed a highly selective method for mapping the PtdIns(4,5)P2 distribution within cells at high resolution, and our data provide direct evidence for this lipid at key functional locations.

show abstract

Section: Discussionsupporting

confidence: 92%

Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C δ1

Watt

Kular

Fleming

et al. 2002

Biochemical Journal

247

View full text Add to dashboard Cite

show abstract

“…The physiological function(s) of the cytoskeletal Ptdlns 4-kinase in plants is not yet clear. Subcellular distribution studies in animal cells have shown that PtdlnsP can be synthesized intracellularly before it is translocated to the plasma membrane, where it is further phosphorylated to Ptdlns(4,5)P2 (Lundberg and Jergil, 1988). Although the main intracellular nonplasma membrane site for PtdlnsP formation in certain mammalian cells appears to be membranous (Olsson et al, 1991), the cytoskeletal Ptdlns 4-kinase may nevertheless similarly provide Ptdlns(4)P for translocation.…”

Section: Discussionmentioning

confidence: 99%

Association of Phosphatidylinositol 4-Kinase with the Plant Cytoskeleton

Xu¹,

Lloyd²,

Staiger³

et al. 1992

The Plant Cell

View full text Add to dashboard Cite

In eukaryotic cells, phosphatidylinositol 4-hydroxy kinase and phosphatidylinositol-4-phosphate 5-hydroxy kinase are responsible for the formation of the two second messenger precursors phosphatidylinositol-4-phosphate (Ptdlns(4)P) and phosphatidylinositol-4,5-bisphosphate (Ptdlns(4,5)P2). In plant cells, these kinases have been considered to be exclusively membrane associated, with the majority of activity residing in the inner leaflet of the plasmalemma. By sequentially extracting carrot protoplasts with the detergent Nonidet P-40 then more rigorously with Triton X-100, we were able to remove the activity of three separate plasma membrane marker enzymes and to demonstrate that a significant proportion of cellular Ptdlns 4-kinase is associated with the cytoskeleton. When only endogenous substrates were present, Nonidet P-40-permeabilized protoplasts and Nonidet P-40-extracted cytoskeletons displayed a pattern of lipid phosphorylation similar to that obtained with isolated plant membranes or permeabilized cells, whereas the Triton X-100-extracted cytoskeletons showed little or no activity. In contrast, when exogenous substrates were added, a major proportion of PtdlnsP formed was due to kinase activity associated with the cytoskeleton as well as nuclei. However, by subtracting the activity of isolated nuclei, it could be demonstrated that a significant proportion of the detergent-resistant Ptdlns kinase activity resides with the cytoskeletal fraction. These findings suggest that the pathways of polyphosphoinositide biosynthesis in plant cells should be reevaluated to take account of the cytoskeleton and that Ptdlns(4)P itself may play a unique role in modulation of plant cytoskeletal integrity and cellular signal transduction.

show abstract

“…Wong et al (25) reported that PI 4-kinase ␣ is localized in the ER, whereas PI 4-kinase ␤ is localized in the Golgi apparatus in HeLa cells. Most PI synthase activity is also detected in the ER (24,26,27). It is conceivable that PI(4,5)P 2 synthesis occurs efficiently in microsomes because of the relay of substrates between PI synthase, PI kinase, and PIPK.…”

Section: Phosphatidylinositol-5-phosphate 4-kinasementioning

confidence: 99%

A Novel Phosphatidylinositol-5-phosphate 4-Kinase (Phosphatidylinositol-phosphate Kinase IIγ) Is Phosphorylated in the Endoplasmic Reticulum in Response to Mitogenic Signals

Itoh

Ijuin

Takenawa

1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

Here, we identify a novel rat phosphatidylinositol-5-phosphate 4-kinase, phosphatidylinositol-phosphate kinase II␥ (PIPKII␥ Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P 2 ) 1 is a phospholipid with a variety of functions in vivo including not only the production of second messengers such as diacylglycerol and inositol 1,4,5-trisphosphate, but also the regulation of actin regulatory proteins and the activation of phospholipase D and ADP-ribosylation factor. It has also been reported that PI(4,5)P 2 synthesis is potentiated by various stimuli including GTP␥S (1-3), phorbol esters (4), tyrosine kinases (5), and integrins (6). The variations in its function and the regulation of its synthesis indicate that enzymes responsible for the production of PIP 2 , such as PI kinase and PIPK, also show large diversities. Among PIPKs, two major subtypes (types I and II), each comprising two isoforms (I␣, I␤, II␣, and II␤), have been identified to date (13, 16 -18), and it is thought that the role for each subtype in vivo is different. The type

show abstract

Generation of phosphatidylinositol 4,5‐bisphosphate proceeds through an intracellular route in rat hepatocytes

Cited by 29 publications

References 26 publications

Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C δ1

Subcellular localization of phosphatidylinositol 4,5-bisphosphate using the pleckstrin homology domain of phospholipase C δ1

Association of Phosphatidylinositol 4-Kinase with the Plant Cytoskeleton

A Novel Phosphatidylinositol-5-phosphate 4-Kinase (Phosphatidylinositol-phosphate Kinase IIγ) Is Phosphorylated in the Endoplasmic Reticulum in Response to Mitogenic Signals

Contact Info

Product

Resources

About