New insight into the intracellular roles of class II phosphoinositide 3-kinases

2014 ◽  
Vol 42 (5) ◽  
pp. 1378-1382 ◽  
Author(s):  
Tania Maffucci ◽  
Marco Falasca
Keyword(s):  
Class Ii ◽  
Present Review ◽  
Phosphoinositide 3 Kinase ◽  
Redundant Role ◽  
Insight Into

In the last few years, an increased attention to class II isoforms of phosphoinositide 3-kinase (PI3K) has emerged, mainly fuelled by evidence suggesting a distinct non-redundant role for these enzymes compared with other PI3Ks. Despite this renewed interest, many questions remain on the specific functions regulated by these isoforms and their mechanism of activation and action. In the present review, we discuss results from recent studies that have provided some answers to these questions.

Regulation and cellular functions of class II phosphoinositide 3-kinases

2012 ◽  
Vol 443 (3) ◽  
pp. 587-601 ◽  
Author(s):  
Marco Falasca ◽  
Tania Maffucci
Keyword(s):  
Class Ii ◽  
Human Diseases ◽  
Present Review ◽  
Signalling Pathways ◽  
Cellular Functions ◽  
Functional Roles ◽  
Physiological Processes ◽  
Pathological Conditions ◽  
Downstream Effectors ◽  
Phosphoinositide 3 Kinase

Class II isoforms of PI3K (phosphoinositide 3-kinase) are still the least investigated and characterized of all PI3Ks. In the last few years, an increased interest in these enzymes has improved our understanding of their cellular functions. However, several questions still remain unanswered on their mechanisms of activation, their specific downstream effectors and their contribution to physiological processes and pathological conditions. Emerging evidence suggests that distinct PI3Ks activate different signalling pathways, indicating that their functional roles are probably not redundant. In the present review, we discuss the recent advances in our understanding of mammalian class II PI3Ks and the evidence suggesting their involvement in human diseases.

scholarly journals A Brief Insight into Microbial Corrosion and its Mitigation with Eco-friendly Inhibitors

2021 ◽  
Vol 7 (3) ◽  
Author(s):  
M. Lavanya
Keyword(s):  
Electrochemical Impedance ◽  
Wide Spectrum ◽  
Present Review ◽  
Electrochemical Reactions ◽  
Microbial Corrosion ◽  
Engineering Applications ◽  
Microbially Influenced Corrosion ◽  
Catastrophic Failures ◽  
Chemical Strategies ◽  
Insight Into

AbstractCorrosion results from the electrochemical reactions between the metal and its existing environment. Corrosion results in severe and expensive damage to a wide spectrum of industries. When microbes are involved in corrosion it is seldom possible to economically evaluate its impact. Microbially influenced corrosion is recognized to cause catastrophic failures contributing to approximately 20% of the annual losses. In many engineering applications, microbially influenced corrosion control is of prime importance. Expensive, toxicity and sometimes, even ineffectiveness of the current chemical strategies to mitigate microbially influenced corrosion have shifted the interest towards eco-friendly inhibitors. The present review discusses microbial induced corrosion in various metals and its inhibition through eco-friendly inhibitors. In addition, the study also reviews the morphological and electrochemical impedance results.

scholarly journals Fractionation and Characterization of Petroleum Asphaltene: Focus on Metalopetroleomics

Processes ◽  
2020 ◽  
Vol 8 (11) ◽  
pp. 1504
Author(s):  
Fang Zheng ◽  
Quan Shi ◽  
Germain Salvato Vallverdu ◽  
Pierre Giusti ◽  
Brice Bouyssiere
Keyword(s):  
Analytical Techniques ◽  
Review Article ◽  
Polar Fraction ◽  
Present Review ◽  
Current Review ◽  
Future Work ◽  
Insight Into

Asphaltenes, as the heaviest and most polar fraction of petroleum, have been characterized by various analytical techniques. A variety of fractionation methods have been carried out to separate asphaltenes into multiple subfractions for further investigation, and some of them have important reference significance. The goal of the current review article is to offer insight into the multitudinous analytical techniques and fractionation methods of asphaltene analysis, following an introduction with regard to the morphologies of metals and heteroatoms in asphaltenes, as well their functions on asphaltene aggregation. Learned lessons and suggestions on possible future work conclude the present review article.

Ablation of phosphoinositide-3-kinase class II alpha suppresses hepatoma cell proliferation

2009 ◽  
Vol 387 (2) ◽  
pp. 310-315 ◽  
Author(s):  
Stanley K.L. Ng ◽  
Soek-Ying Neo ◽  
Yann-Wan Yap ◽  
R. Krishna Murthy Karuturi ◽  
Evelyn S.L. Loh ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Hepatoma Cell ◽  
Class Ii ◽  
Phosphoinositide 3 Kinase ◽  
Class Ii Alpha

scholarly journals The Class II Phosphoinositide 3-Kinase C2β Is Not Essential for Epidermal Differentiation

2005 ◽  
Vol 25 (24) ◽  
pp. 11122-11130 ◽  
Author(s):  
Kazutoshi Harada ◽  
Amy B. Truong ◽  
Ti Cai ◽  
Paul A. Khavari
Keyword(s):  
Class Ii ◽  
Epidermal Cells ◽  
Epidermal Differentiation ◽  
Class I ◽  
Differentiation Markers ◽  
Cellular Processes ◽  
Targeted Gene Deletion ◽  
Epidermal Growth ◽  
Phosphoinositide 3 Kinase

ABSTRACT Phosphoinositide 3-kinases (PI3Ks) regulate an array of cellular processes and are comprised of three classes. Class I PI3Ks include the well-studied agonist-sensitive p110 isoforms; however, the functions of class II and III PI3Ks are less well characterized. Of the three class II PI3Ks, C2α and C2β are widely expressed in many tissues, including the epidermis, while C2γ is confined to the liver. In contrast to the class I PI3K p110α, which is expressed throughout the epidermis, C2β was found to be localized in suprabasal cells, suggesting a potential role for C2β in epidermal differentiation. Overexpressing C2β in epidermal cells in vitro induced differentiation markers. To study a role for C2β in tissue, we generated transgenic mice overexpressing C2β in both suprabasal and basal epidermal layers. These mice lacked epidermal abnormalities. Mice deficient in C2β were then generated by targeted gene deletion. C2β knockout mice were viable and fertile and displayed normal epidermal growth, differentiation, barrier function, and wound healing. To exclude compensation by C2α, RNA interference was then used to knock down both C2α and C2β in epidermal cells simultaneously. Induction of differentiation markers was unaffected in the absence of C2α and C2β. These findings indicate that class II PI3Ks are not essential for epidermal differentiation.

Epidermal growth factor stimulates translocation of the class II phosphoinositide 3-kinase PI3K-C2β to the nucleus

2009 ◽  
Vol 422 (1) ◽  
pp. 53-60 ◽  
Author(s):  
Hrvoje Banfic ◽  
Dora Visnjic ◽  
Nikica Mise ◽  
Sanjeevi Balakrishnan ◽  
Simona Deplano ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Nuclear Localization ◽  
Mammalian Cells ◽  
Class Ii ◽  
Kinase Assay ◽  
C2 Domain ◽  
Protein Fusion ◽  
Epidermal Growth ◽  
Phosphoinositide 3 Kinase

Although the class II phosphoinositide 3-kinase enzymes PI3K-C2α and PI3K-C2β act acutely downstream of cell surface receptors they have also been localized to nuclei in mammalian cells. As with the class I PI3K enzymes, the relationship between the pools of enzyme present in cytoplasm and nuclei remains poorly understood. In this study we test the hypothesis that PI3K-C2β translocates to nuclei in response to growth factor stimulation. Fractionating homogenates of quiescent cells revealed that less than 5% of total PI3K-C2β resides in nuclei. Stimulation with epidermal growth factor sequentially increased levels of this enzyme, firstly in the cytosol and secondly in the nuclei. Using detergent-treated nuclei, we showed that PI3K-C2β co-localized with lamin A/C in the nuclear matrix. This was confirmed biochemically, and a phosphoinositide kinase assay showed a statistically significant increase in nuclear PI3K-C2β levels and lipid kinase activity following epidermal growth factor stimulation. C-terminal deletion and point mutations of PI3K-C2β demonstrated that epidermal growth factor-driven translocation to the nucleus is dependent on a sequence of basic amino acid residues (KxKxK) that form a nuclear localization motif within the C-terminal C2 domain. Furthermore, when this sequence was expressed as an EGFP (enhanced green fluorescent protein) fusion protein, it translocated fluorescence into nuclei with an efficiency dependent upon copy number. These data demonstrate that epidermal growth factor stimulates the appearance of PI3K-C2β in nuclei. Further, this effect is dependent on a nuclear localization signal present within the C-terminal C2 domain, indicating its bimodal function regulating phospholipid binding and shuttling PI3K-C2β into the nucleus.

Cloning and Characterization of a Novel Class II Phosphoinositide 3-Kinase Containing C2 Domain

1998 ◽  
Vol 244 (2) ◽  
pp. 531-539 ◽  
Author(s):  
Hiroyuki Misawa ◽  
Motoaki Ohtsubo ◽  
Neal G. Copeland ◽  
Debra J. Gilbert ◽  
Nancy A. Jenkins ◽  
...  
Keyword(s):  
Class Ii ◽  
C2 Domain ◽  
Phosphoinositide 3 Kinase
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