A short history of inositol lipids

Irvine, Robin F.

doi:10.1194/jlr.r071712

Cited by 33 publications

(21 citation statements)

References 91 publications

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“…Mono-PIs were initially considered as mere biosynthetic precursors of more complex PIs such as PI(4,5)-bisphosphate (PI(4,5)P 2 ). However, it is now becoming apparent that they play signaling roles as second messengers in a number of physiological and pathological processes [1][2][3]. For example, recent results have shown that PI5P conveys compartmentalized signals at the plasma membrane, endocytic membranes, and the nucleus in several cell types [1,2,[4][5][6][7][8][9].…”

Section: Introductionmentioning

confidence: 99%

“…However, it is now becoming apparent that they play signaling roles as second messengers in a number of physiological and pathological processes [1][2][3]. For example, recent results have shown that PI5P conveys compartmentalized signals at the plasma membrane, endocytic membranes, and the nucleus in several cell types [1,2,[4][5][6][7][8][9]. The effects of these lipids are relayed via the interaction with intracellular targets bearing specialized PI-binding regions such as the pleckstrin homology (PH), plant homeodomain (PHD), Vps27-Hrs-Stam (VHS), Phox homology (PX), and Fab1-Yotb-Vac1-EEA1 (FYVE) domains [2,10].…”

Section: Introductionmentioning

confidence: 99%

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Phosphatidylinositol Monophosphates Regulate Optimal Vav1 Signaling Output

Rodríguez-Fdez

Citterio

Lorenzo‐Martín

et al. 2019

Cells

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Phosphatidylinositol–5 phosphate (PI5P) and other mono-phosphoinositides (mono-PIs) play second messenger roles in both physiological and pathological conditions. Despite this, their intracellular targets and mechanisms of action remain poorly characterized. Here, we show that Vav1, a protein that exhibits both Rac1 GDP/GTP exchange and adaptor activities, is positively modulated by PI5P and, possibly, other mono-PIs. Unlike other phospholipid–protein complexes, the affinity and specificity of the Vav1–lipid interaction entail a new structural solution that involves the synergistic action of the Vav1 C1 domain and an adjacent polybasic tail. This new regulatory layer, which is not conserved in the Vav family paralogs, favors the engagement of optimal Vav1 signaling outputs in lymphocytes.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Phosphatidylinositol Monophosphates Regulate Optimal Vav1 Signaling Output

Rodríguez-Fdez

Citterio

Lorenzo‐Martín

et al. 2019

Cells

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“…Many PIs are overall in low abundance in the membrane but they can be found at high local concentrations in membrane domains not readily detected by conventional techniques [ 3 , 17 ]. For a historical review on inositol lipids, see Irvine (2016) [ 18 ]. Over the last couple of decades, PIs have been found to be one of the most ubiquitous signaling entities in eukaryotic metabolism.…”

Section: The Phosphoinositide Familymentioning

confidence: 99%

Structure and Lateral Organization of Phosphatidylinositol 4,5-bisphosphate

Borges-Araújo

Fernandes

2020

Molecules

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Phosphatidylinositol 4,5- bisphosphate (PI(4,5)P2) is a minor but ubiquitous component of the inner leaflet of the plasma membrane of eukaryotic cells. However, due to its particular complex biophysical properties, it stands out from its neighboring lipids as one of the most important regulators of membrane-associated signaling events. Despite its very low steady-state concentration, PI(4,5)P2 is able to engage in a multitude of simultaneous cellular functions that are temporally and spatially regulated through the presence of localized transient pools of PI(4,5)P2 in the membrane. These pools are crucial for the recruitment, activation, and organization of signaling proteins and consequent regulation of downstream signaling. The present review showcases some of the most important PI(4,5)P2 molecular and biophysical properties as well as their impact on its membrane dynamics, lateral organization, and interactions with other biochemical partners.

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“…Consequently, the activation of phosphorylating enzymes also produced by the increase in [Ca 2+ ]i fosters biochemical processes that go in the opposite direction to the reactions of the catalyzed hydrolysis of the phospholipases and phosphatases as described above. The action of phosphatidyl inositol phosphate kinase (PIPK) opposes that of PLC [Sun 2013], whilst the various kinases control the phosphatases by the synthesis of an array of inositol trisphosphate (IP3) and tetrakisphosphate (IP4) molecules in the cytosol [Irvine 2001, Shears 2004, Bunney 2010, Irvine 2016, Anguita 2018. The opposing action must take place rapidly and with sufficient force, conditions guaranteed by the fact that phosphorylating enzymes are no less Ca 2+ -dependent than the phospholipases and phosphatases.…”

Section: Control and Feedbackmentioning

confidence: 99%

Role of Protons in Calcium Signaling

Molinari¹,

Nervo²

2020

Preprint

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36 years after the publication of the important article by Busa and Nuccitelli on the variability of intracellular pH (pHi) and the interdependence of pHi and intracellular Ca2+ concentration ([Ca2+]i), little research has been carried out on pHi and calcium signaling. Moreover, the results appear to be contradictory. Some authors claim that the increase in [Ca2+]i is due to a reduction in pHi, others that it is caused by an increase in pHi. The reasons for these conflicting results have not yet been discussed and clarified in an exhaustive manner. Variations in pHi have a significant impact on the increase in [Ca2+]i and hence on some of the basic biochemical mechanisms of calcium signaling. This paper focuses on the possible triggering role of protons, highlighting the mechanisms potentially involved and the open issues that could be clarified by research.

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A short history of inositol lipids

Cited by 33 publications

References 91 publications

Phosphatidylinositol Monophosphates Regulate Optimal Vav1 Signaling Output

Phosphatidylinositol Monophosphates Regulate Optimal Vav1 Signaling Output

Structure and Lateral Organization of Phosphatidylinositol 4,5-bisphosphate

Role of Protons in Calcium Signaling

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