Results 41 to 50 of about 58,639 (259)

CO2 Transport by PIP2 Aquaporins of Barley [PDF]

open access: yesPlant and Cell Physiology, 2014
CO2 permeability of plasma membrane intrinsic protein 2 (PIP2) aquaporins of Hordeum vulgare L. was investigated. Five PIP2 members were heterologously expressed in Xenopus laevis oocytes. CO2 permeability was determined by decrease of cytosolic pH in CO2-enriched buffer using a hydrogen ion-selective microelectrode.
Mori, Izumi C.   +6 more
openaire   +2 more sources

Charge Shielding of PIP2 by Cations Regulates Enzyme Activity of Phospholipase C.

open access: yesPLoS ONE, 2015
Hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) of the plasma membrane by phospholipase C (PLC) generates two critical second messengers, inositol-1,4,5-trisphosphate and diacylglycerol.
Jong Bae Seo   +4 more
doaj   +1 more source

Structural basis of control of inward rectifier Kir2 channel gating by bulk anionic phospholipids [PDF]

open access: yes, 2016
Inward rectifier potassium (Kir) channel activity is controlled by plasma membrane lipids. Phosphatidylinositol-4,5-bisphosphate (PIP(2)) binding to a primary site is required for opening of classic inward rectifier Kir2.1 and Kir2.2 channels, but ...
Anna Stary-Weinzinger   +55 more
core   +2 more sources

PIP2 PIP2 Hooray for Maxi K+ [PDF]

open access: yesThe Journal of General Physiology, 2008
Voltage-gated K+ (KV) channels contain a voltage-sensing transmembrane segment that moves in response to changes in membrane potential. A small “gating” current arises from the translocation of positively charged residues within the channel's voltage sensor.
openaire   +3 more sources

Synthetic Manipulation of PIP2 Levels and PIP2-Associated Chemotactic Signaling Dissection in Dictyostelium [PDF]

open access: yesBiophysical Journal, 2015
Phosphatidylinositol 4,5-bisphosphate (PIP2) has been shown involved in key chemotactic signaling pathways in Dictyostelium, but our understanding of its roles in this signaling network is very limited. To explore the hypothesis that PIP2 negatively regulate chemotactic signaling events, we used the Chemically-induced Dimerization system, which allows ...
Miao, Yuchuan   +2 more
openaire   +1 more source

A dPIP5K dependent pool of phosphatidylinositol 4,5 bisphosphate (PIP2) is required for G-protein coupled signal transduction in Drosophila photoreceptors.

open access: yesPLoS Genetics, 2015
Multiple PIP2 dependent molecular processes including receptor activated phospholipase C activity occur at the neuronal plasma membranes, yet levels of this lipid at the plasma membrane are remarkably stable.
Purbani Chakrabarti   +6 more
doaj   +1 more source

Lipid kinase PIP5Kα contributes to Hippo pathway activation via interaction with Merlin and by mediating plasma membrane targeting of LATS1

open access: yesCell Communication and Signaling, 2023
Background The Hippo pathway plays a critical role in controlled cell proliferation. The tumor suppressor Merlin and large tumor suppressor kinase 1 (LATS1) mediate activation of Hippo pathway, consequently inhibiting the primary effectors, Yes ...
Truc Phan Hoang Le   +4 more
doaj   +1 more source

Dual Regulation of Voltage-Sensitive Ion Channels by PIP2

open access: yesFrontiers in Pharmacology, 2012
Over the past 16 years, there has been an impressive number of ion channels shown to be sensitive to the major phosphoinositide in the plasma membrane, phosphatidilinositol 4,5-bisphosphate (PIP2). Among them are voltage-gated channels, which are crucial
Aldo A Rodríguez Menchaca   +3 more
doaj   +1 more source

The biphasic increase of PIP2 in the fertilized eggs of starfish: new roles in actin polymerization and Ca2+ signaling. [PDF]

open access: yesPLoS ONE, 2010
BACKGROUND: Fertilization of echinoderm eggs is accompanied by dynamic changes of the actin cytoskeleton and by a drastic increase of cytosolic Ca(2+). Since the plasma membrane-enriched phospholipid phosphatidylinositol 4,5-bisphosphate (PIP2) serves as
Jong T Chun   +5 more
doaj   +1 more source

Stereociliary Myosin-1c Receptors Are Sensitive to Calcium Chelation and Absent from Cadherin 23 Mutant Mice [PDF]

open access: yes, 2006
The identities of some of the constituents of the hair-cell transduction apparatus have been elucidated only recently. The molecular motor myosin-1c (Myo1c) functions in adaptation of the hair-cell response to sustained mechanical stimuli and is ...
Cyr, Janet L   +4 more
core   +1 more source

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