Results 11 to 20 of about 707,375 (141)

Ion channel regulation by phosphoinositides analyzed with VSPs – PI(4,5)P2 affinity, phosphoinositide selectivity, and PI(4,5)P2 pool accessibility

open access: yesFrontiers in Pharmacology, 2015
The activity of many proteins depends on the phosphoinositide (PI) content of the membrane. E.g., dynamic changes of the concentration of PI(4,5)P2 are cellular signals that regulate ion channels.
Alexandra eRjasanow   +4 more
doaj   +2 more sources

The PI(3,5)P2 and PI(4,5)P2 Interactomes

open access: yes, 2016
A comprehensive analysis of the phosphoinositide interactome has been performed using analogues of PI(3,5)P2 and PI(4,5)P2 phosphatidyl phospholipids which were immobilized onto Affi-10 beads or incorporated into liposomes for use as affinity absorbents ...
Lisa Connolly (2405047)   +8 more
core   +12 more sources

Interaction between the Lentil Lipid Transfer Protein Lc-LTP2 and Its Novel Signal Ligand PI(4,5)P2 [PDF]

open access: yesMembranes, 2020
It is known that plant lipid transfer proteins (LTPs) bind a broad spectrum of ligands including fatty acids (FAs), phospho- and glycolipids, acyl-coenzyme A and secondary metabolites.
Daria Melnikova   +3 more
doaj   +2 more sources

PI(4,5)P2 binding sites in the Ebola virus matrix protein VP40 modulate assembly and budding [PDF]

open access: yesJournal of Lipid Research
Ebola virus (EBOV) causes severe hemorrhagic fever in humans and is lethal in a large percentage of those infected. The EBOV matrix protein viral protein 40 kDa (VP40) is a peripheral binding protein that forms a shell beneath the lipid bilayer in ...
Kristen A. Johnson   +8 more
doaj   +2 more sources

A novel homeostatic mechanism tunes PI(4,5)P2-dependent signaling at the plasma membrane.

open access: yesJ Cell Sci, 2023
The lipid molecule phosphatidylinositol (4,5)-bisphosphate (PI(4,5)P2) controls virtually all aspects of plasma membrane (PM) function in animal cells. These functions range from cellular signaling to selective membrane permeability to the attachment of ...
Wills RC   +5 more
europepmc   +2 more sources

Two cooperative binding sites sensitize PI(4,5)P2 recognition by the tubby domain. [PDF]

open access: yesSci Adv, 2022
Phosphoinositides (PIs) are lipid signaling molecules that operate by recruiting proteins to cellular membranes via PI recognition domains. The dominant PI of the plasma membrane is phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2].
Thallmair V   +5 more
europepmc   +3 more sources

A positive feedback loop between Flower and PI(4,5)P2 at periactive zones controls bulk endocytosis in Drosophila

open access: yeseLife, 2020
Synaptic vesicle (SV) endocytosis is coupled to exocytosis to maintain SV pool size and thus neurotransmitter release. Intense stimulation induces activity-dependent bulk endocytosis (ADBE) to recapture large quantities of SV constituents in large ...
Tsai-Ning Li   +5 more
doaj   +1 more source

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

Home - About - Disclaimer - Privacy