Results 21 to 30 of about 20,725 (233)

From lipid modification to cell death: the diverse roles of S-palmitoylation in cell fate decisions. [PDF]

open access: yesCell Commun Signal
S-palmitoylation is a dynamic, reversible lipid modification that plays a crucial role in the regulation of various types of cell death. However, systematic insights into how S-palmitoylation modifications integrate and mediate crosstalk among diverse ...
Zhu Y   +5 more
europepmc   +2 more sources

The role of protein palmitoylation in disease pathogenesis and therapeutic innovation. [PDF]

open access: yesAnn Med
Background Protein palmitoylation is a significant post-translational modification that influences protein stability, localization, and signaling through the addition of palmitoyl groups to cysteine, serine/threonine, or lysine residues.
Lin X   +7 more
europepmc   +2 more sources

Post-translational palmitoylation of metabolic proteins

open access: yesFrontiers in Physiology, 2023
Numerous cellular proteins are post-translationally modified by addition of a lipid group to their structure, which dynamically influences the proteome by increasing hydrophobicity of proteins often impacting protein conformation, localization, stability,
Kaitlyn M. J. H. Dennis, Lisa C. Heather
doaj   +3 more sources

Palmitoylation-dependent regulation of GPX4 suppresses ferroptosis

open access: yesNature Communications
S-palmitoylation is a reversible and widespread post-translational modification, but its role in the regulation of ferroptosis has been poorly understood. Here, we elucidate that GPX4, an essential regulator of ferroptosis, is reversibly palmitoylated on
Bin Huang   +10 more
doaj   +2 more sources

The role of palmitoylation in signalling, cellular trafficking and plasma membrane localization of protease-activated receptor-2.

open access: yesPLoS ONE, 2011
Protease-activated receptor-2 (PAR2) is a G protein coupled receptor (GPCR) activated by proteolytic cleavage of its amino terminal domain by trypsin-like serine proteases. This irreversible activation mechanism leads to rapid receptor desensitization by
Mark N Adams   +4 more
doaj   +2 more sources

Role of Palmitoylation of Postsynaptic Proteins in Promoting Synaptic Plasticity [PDF]

open access: yesFrontiers in Molecular Neuroscience, 2019
Many postsynaptic proteins undergo palmitoylation, the reversible attachment of the fatty acid palmitate to cysteine residues, which influences trafficking, localization, and protein interaction dynamics.
Lucas Matt   +3 more
doaj   +2 more sources

Palmitoylation as a Functional Regulator of Neurotransmitter Receptors

open access: yesNeural Plasticity, 2018
The majority of neuronal proteins involved in cellular signaling undergo different posttranslational modifications significantly affecting their functions.
Vladimir S. Naumenko, Evgeni Ponimaskin
doaj   +2 more sources

Palmitoylation-Dependent Small-Molecule Fluorescent Probes for Live-Cell Golgi Imaging

open access: yes, 2023
Small-molecule fluorescent probes enabling visualization of the Golgi apparatus in living cells are essential tools for studying Golgi-associated biological processes and diseases.
Emi Mishiro-Sato (14426149)   +13 more
core   +3 more sources

Crosstalk of Synapsin1 palmitoylation and phosphorylation controls the dynamicity of synaptic vesicles in neurons

open access: yesCell Death and Disease, 2022
The dynamics of synaptic vesicles (SVs) within presynaptic domains are tightly controlled by synapsin1 phosphorylation; however, the mechanism underlying the anchoring of synapsin1 with F-actin or SVs is not yet fully understood. Here, we found that Syn1
Peipei Yan   +14 more
doaj   +1 more source

Dynamic but discordant alterations in zDHHC5 expression and palmitoylation of its substrates in cardiac pathologies

open access: yesFrontiers in Physiology, 2022
S-palmitoylation is an essential lipid modification catalysed by zDHHC-palmitoyl acyltransferases that regulates the localisation and activity of substrates in every class of protein and tissue investigated to date.
Alice Main   +11 more
doaj   +1 more source

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