Results 61 to 70 of about 31,206 (230)
CRISPR and Gene Augmentation Rescue Trabecular Meshwork Dysfunction in iPSC Models of Lowe Syndrome
Advanced Science, EarlyView.By modeling Lowe syndrome using patient‐derived iPSCs, this study establishes a human disease model that faithfully recapitulates OCRL deficiency‐associated ciliary and cytoskeletal defects. The model enables evaluation of both mutation‐agnostic DNA augmentation and CRISPR‐mediated mutation correction strategies, both of which restore OCRL function and
Siyu Chen +11 more
wiley +1 more source
Membrane cytoskeleton: PIP2 pulls the strings [PDF]
, 2000 A recent application of optical tweezers has shown that plasma membrane phosphatidylinositol 4,5-bisphosphate (PIP2) levels control adhesion of the membrane bilayer to the underlying cytoskeleton, by regulated direct binding of PIP2 to cytoskeletal ...
Oh, Sang W. +2 more
core +1 more source
Anillin Puts RhoA in Touch with PIP2 [PDF]
Developmental Cell, 2019 In this issue of Developmental Cell, Budnar and colleagues report how the scaffolding protein anillin uses cycles of transient binding interactions to enhance the residence time and signaling output of active RhoA to control actomyosin contractility at epithelial junctions and during cell division.
openaire +2 more sources
Localization of the PIP2 Sensor of TRPV1 Ion Channels [PDF]
Journal of Biological Chemistry, 2011 Although a large number of ion channels are now believed to be regulated by phosphoinositides, particularly phosphoinositide 4,5-bisphosphate (PIP2), the mechanisms involved in phosphoinositide regulation are unclear. For the TRP superfamily of ion channels, the role and mechanism of PIP2 modulation has been especially difficult to resolve. Outstanding
Carmen A, Ufret-Vincenty +4 more
openaire +2 more sources
Novel Phosphotidylinositol 4,5-Bisphosphate Binding Sites on Focal Adhesion Kinase. [PDF]
PLoS ONE, 2015 Focal adhesion kinase (FAK) is a protein tyrosine kinase that is ubiquitously expressed, recruited to focal adhesions, and engages in a variety of cellular signaling pathways.
Jun Feng, Blake Mertz
doaj +1 more source
Inhibition of the proton-activated chloride channel PAC by PIP2
eLife, 2023 Proton-activated chloride (PAC) channel is a ubiquitously expressed pH-sensing ion channel, encoded by PACC1 (TMEM206). PAC regulates endosomal acidification and macropinosome shrinkage by releasing chloride from the organelle lumens. It is also found at
Ljubica Mihaljević +4 more
doaj +1 more source
An Extracellular Pore‑Targeting Peptide Defines a Designable Allosteric Site in TRPV2
Advanced Science, EarlyView.Structure‐guided peptide engineering yields Depiv2, a highly potent and subtype‐selective TRPV2 inhibitor that binds to the extracellular pore and remodels it into a closed, non‐conductive state. Depiv2 suppresses pathological cardiac hypertrophy, establishing the TRPV2 outer pore as a designable interface for selective peptide modulation.
Aiqin Zhu +7 more
wiley +1 more source
Relationship between membrane phosphatidylinositol-4,5-bisphosphate and receptor-mediated inhibition of native neuronal M channels [PDF]
, 2005 The relationship between receptor-induced membrane phosphatidylinositol-4'5'-bisphosphate (PIP2) hydrolysis and M-current inhibition was assessed in single-dissociated rat sympathetic neurons by simultaneous or parallel recording of membrane current and ...
Abogadie, FC +6 more
core
Dual Regulation of Kv1.2 Activation by PIP2 [PDF]
Biophysical Journal, 2011 Phosphatidylinositol (4,5)-bisphosphate is now recognized as a ubiquitous regulator of ion channels and transporters. We report here that PIP2 regulates activation of Kv1.2, a Shaker family voltage-gated potassium channel. In inside-out macropatches of Xenopus laevis oocytes, loss of PIP2 induced a leftward shift in the voltage-dependence of activation
Rodriguez-Menchaca, Aldo A. +2 more
openaire +1 more source
PLoS ONE, 2013 The C2 domain of PKCα possesses two different binding sites, one for Ca(2+) and phosphatidylserine and a second one that binds PIP2 with very high affinity. The enzymatic activity of PKCα was studied by activating it with large unilamellar lipid vesicles,
Antonio L Egea-Jiménez +3 more
doaj +1 more source