Results 31 to 40 of about 62,994 (190)

Membrane-mediated dimerization potentiates PIP5K lipid kinase activity

open access: yeseLife, 2022
The phosphatidylinositol 4-phosphate 5-kinase (PIP5K) family of lipid-modifying enzymes generate the majority of phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] lipids found at the plasma membrane in eukaryotic cells.
Scott D Hansen   +3 more
doaj   +1 more source

Phosphatidylinositol 4,5-bisphosphate optical uncaging potentiates exocytosis

open access: yeseLife, 2017
Phosphatidylinositol-4,5-bisphosphate [PI(4,5)P2] is essential for exocytosis. Classical ways of manipulating PI(4,5)P2 levels are slower than its metabolism, making it difficult to distinguish effects of PI(4,5)P2 from those of its metabolites.
Alexander M Walter   +15 more
doaj   +1 more source

Phospholipid binding to the FAK catalytic domain impacts function. [PDF]

open access: yesPLoS ONE, 2017
Focal adhesion kinase is an essential nonreceptor tyrosine kinase that plays an important role in development, in homeostasis and in the progression of human disease.
Jessica E Hall, Michael D Schaller
doaj   +1 more source

Allosteric stabilization of calcium and phosphoinositide dual binding engages several synaptotagmins in fast exocytosis

open access: yeseLife, 2022
Synaptic communication relies on the fusion of synaptic vesicles with the plasma membrane, which leads to neurotransmitter release. This exocytosis is triggered by brief and local elevations of intracellular Ca2+ with remarkably high sensitivity.
Janus RL Kobbersmed   +4 more
doaj   +1 more source

Structural insights on TRPV5 gating by endogenous modulators. [PDF]

open access: yes, 2018
TRPV5 is a transient receptor potential channel involved in calcium reabsorption. Here we investigate the interaction of two endogenous modulators with TRPV5.
Carnevale, Vincenzo   +13 more
core   +3 more sources

Ca2+ induces PI(4,5)P2 clusters on lipid bilayers at physiological PI(4,5)P2 and Ca2+ concentrations

open access: yesBiochimica et Biophysica Acta (BBA) - Biomembranes, 2014
Calcium has been shown to induce clustering of PI(4,5)P2 at high and non-physiological concentrations of both the divalent ion and the phosphatidylinositol, or on supported lipid monolayers. In lipid bilayers at physiological conditions, clusters are not detected through microscopic techniques.
Sarmento, Maria J.   +4 more
openaire   +2 more sources

Translocation between PI(4,5)P2-Poor and PI(4,5)P2-Rich Microdomains During Store Depletion Determines STIM1 Conformation and Gating of Orai1 [PDF]

open access: yesBiophysical Journal, 2015
Shmuel Muallem1, Jozsef Maleth1,2,4, Seok Choi1,3,4, and Malini Ahuja1From the 1Epithelial Signaling and Transport Section, NIDCR, NIH, Bethesda MD, 20892, 2First Department of Medicine, University of Szeged, Szeged, Hungary, 3Department of Physiology, Chosun University, South KoreaReceptor-stimulated Ca2+ influx, a critical component of the Ca2 ...
Muallem, Shmuel   +3 more
openaire   +5 more sources

Absence of clustering of phosphatidylinositol-(4,5)-bisphosphate in fluid phosphatidylcholine

open access: yesJournal of Lipid Research, 2006
Phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P2] plays a key role in the modulation of actin polymerization and vesicle trafficking. These processes seem to depend on the enrichment of PI(4,5)P2 in plasma membrane domains. Here, we show that PI(4,5)P2
Faébio Fernandes   +3 more
doaj   +1 more source

Gradients of PI(4,5)P2 and PI(3,5)P2 Jointly Participate in Shaping the Back State of Dictyostelium Cells [PDF]

open access: yesFrontiers in Cell and Developmental Biology, 2022
Polarity, which refers to the molecular or structural asymmetry in cells, is essential for diverse cellular functions. Dictyostelium has proven to be a valuable system for dissecting the molecular mechanisms of cell polarity. Previous studies in Dictyostelium have revealed a range of signaling and cytoskeletal proteins that function at the leading edge
Dong Li   +8 more
openaire   +5 more sources

Topological organisation of the phosphatidylinositol 4,5-bisphosphate-phospholipase C resynthesis cycle: PITPs bridge the ER-PM gap [PDF]

open access: yes, 2016
Phospholipase C (PLC) is a receptor-regulated enzyme that hydrolyses phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) at the plasma membrane (PM) triggering three biochemical consequences, the generation of soluble inositol 1,4,5-trisphosphate (IP3 ...
Cockcroft, S, Raghu, P
core   +1 more source

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