Results 21 to 30 of about 37,335 (238)

S-acylation by ZDHHC20 targets ORAI1 channels to lipid rafts for efficient Ca2+ signaling by Jurkat T cell receptors at the immune synapse

eLife, 2021
Efficient immune responses require Ca2+ fluxes across ORAI1 channels during engagement of T cell receptors (TCR) at the immune synapse (IS) between T cells and antigen presenting cells. Here, we show that ZDHHC20-mediated S-acylation of the ORAI1 channel
Amado Carreras-Sureda, Laurence Abrami, Kim Ji-Hee, Wen-An Wang, Christopher Henry, Maud Frieden, Monica Didier, F Gisou van der Goot, Nicolas Demaurex   +8 more
doaj   +1 more source

Fat traffic control: S-acylation in axonal transport. [PDF]

Mol Pharmacol
Neuronal axons serve as a conduit for the coordinated transport of essential molecular cargo between structurally and functionally distinct subcellular compartments via axonal molecular machinery. Long-distance, efficient axonal transport of membrane-bound organelles enables signal transduction and neuronal homeostasis.
Doerksen AH, Herath NN, Sanders SS.
europepmc   +3 more sources

Palmitoylation: A Fatty Regulator of Myocardial Electrophysiology

Frontiers in Physiology, 2020
Regulation of cardiac physiology is well known to occur through the action of kinases that reversibly phosphorylate ion channels, calcium handling machinery, and signaling effectors.
Kobina Essandoh, Julie M. Philippe, Paul M. Jenkins, Paul M. Jenkins, Matthew J. Brody, Matthew J. Brody   +5 more
doaj   +1 more source

Dynamic Protein S-Acylation in Plants [PDF]

International Journal of Molecular Sciences, 2019
Lipid modification is an important post-translational modification. S-acylation is unique among lipid modifications, as it is reversible and has thus attracted much attention. We summarize some proteins that have been shown experimentally to be S-acylated in plants. Two of these S-acylated proteins have been matched to the S-acyl transferase.
Lihua Zheng, Peng Liu, Qianwen Liu, Tao Wang, Jiangli Dong   +4 more
openaire   +2 more sources

Site-specific analysis of protein S-acylation by resin-assisted capture[S]

Journal of Lipid Research, 2011
Protein S-acylation is a major posttranslational modification whereby a cysteine thiol is converted to a thioester. A prototype is S-palmitoylation (fatty acylation), in which a protein undergoes acylation with a hydrophobic 16 carbon lipid chain ...
Michael T. Forrester, Douglas T. Hess, J. Will Thompson, Rainbo Hultman, M. Arthur Moseley, Jonathan S. Stamler, Patrick J. Casey   +6 more
doaj   +1 more source

Assaying protein palmitoylation in plants

Plant Methods, 2008
Background Protein S-acylation (also known as palmitoylation) is the reversible post-translational addition of acyl lipids to cysteine residues in proteins through a thioester bond. It allows strong association with membranes.
Taylor Laura, Hemsley Piers A, Grierson Claire S   +2 more
doaj   +1 more source

Distinct Roles of N-Terminal Fatty Acid Acylation of the Salinity-Sensor Protein SOS3

Frontiers in Plant Science, 2021
The Salt-Overly-Sensitive (SOS) pathway controls the net uptake of sodium by roots and the xylematic transfer to shoots in vascular plants. SOS3/CBL4 is a core component of the SOS pathway that senses calcium signaling of salinity stress to activate and ...
Irene Villalta, Elena García, Dámaso Hornero-Mendez, Raúl Carranco, Carlos Tello, Imelda Mendoza, Anna De Luca, Zaida Andrés, Karin Schumacher, José M. Pardo, Francisco J. Quintero   +10 more
doaj   +1 more source

The Physiology of ProteinS-acylation [PDF]

Physiological Reviews, 2015
Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is emerging as a ubiquitous mechanism to control the properties and function of a diverse array of proteins and consequently physiological processes. S-acylation results from the enzymatic addition of long-chain lipids, most typically palmitate, onto ...
Chamberlain, Luke H., Shipston, Michael J.   +1 more
openaire   +5 more sources

S-acylation in plants: an expanding field [PDF]

Biochemical Society Transactions, 2020
S-acylation is a common yet poorly understood fatty acid-based post-translational modification of proteins in all eukaryotes, including plants. While exact roles for S-acylation in protein function are largely unknown the reversibility of S-acylation indicates that it is likely able to play a regulatory role.
openaire   +3 more sources

S-acylation regulates the membrane association and activity of Calpain-5 [PDF]

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2022
Abstract Calpain-5 (CAPN5) is a member of the calpain family of calcium-activated neutral thiol proteases. CAPN5 is partly membrane associated, despite its lack of a transmembrane domain. Unlike classical calpains, CAPN5 contains a C-terminal C2 domain. C2 domains often have affinity to lipids, mediating membrane association.
Jozsef, Gal, Vimala, Bondada, Charles B, Mashburn, David W, Rodgers, Dorothy E, Croall, James W, Geddes   +5 more
openaire   +2 more sources