Results 141 to 150 of about 21,089,371 (171)

Protein S-palmitoylation and cancer

Biochimica et Biophysica Acta (BBA) - Reviews on Cancer, 2015
Protein S-palmitoylation is a reversible posttranslational modification of proteins with fatty acids, an enzymatic process driven by a recently discovered family of protein acyltransferases (PATs) that are defined by a conserved catalytic domain characterized by a DHHC sequence motif.
Marc, Yeste-Velasco, Maurine E, Linder, Yong-Jie, Lu   +2 more
openaire   +2 more sources

Position of Proline Mediates the Reactivity of S-Palmitoylation

ACS Chemical Biology, 2015
Palmitoylation, a post-translational modification in which a saturated 16-carbon chain is added predominantly to a cysteine residue, participates in various biological functions. The position of proline relative to other residues being post-translationally modified has been previously reported as being important.
Neelam, Khanal, Vikas, Pejaver, Zhiyu, Li, Predrag, Radivojac, David E, Clemmer, Suchetana, Mukhopadhyay   +5 more
openaire   +2 more sources

Dynamic Radiolabeling of S-Palmitoylated Proteins

2019
Proteins can be radiolabeled either during synthesis, typically using 35S-cysteine/methionine (35S-Cys/Met), or after synthesis, by adding a radiolabeled posttranslational modification. Here we describe how protein S-palmitoylation, and its dynamics, can be monitored by 3H-palmitate labeling and how the importance of S-palmitoylation in protein ...
Abrami L, Denhardt-Eriksson RA, Hatzimanikatis V, van der Goot FG   +3 more
openaire   +3 more sources

S-Palmitoylation Sorts Membrane Cargo for Anterograde Transport in the Golgi [PDF]

Developmental Cell, 2018
While retrograde cargo selection in the Golgi is known to depend on specific signals, it is unknown whether anterograde cargo is sorted, and anterograde signals have not been identified. We suggest here that S-palmitoylation of anterograde cargo at the Golgi membrane interface is an anterograde signal and that it results in concentration in curved ...
Andreas M Ernst, Gregory Lavieu, Aleksander A Rebane   +2 more
exaly   +5 more sources

SwissPalm 2: Protein S-Palmitoylation Database

2019
Protein S-palmitoylation is increasingly recognized as an important posttranslational modification, present in all eukaryotic organisms, involved in the regulation of many biological processes. The SwissPalm database centralizes the large and increasing number of published palmitoyl-proteome datasets, provides tools to compare them, and includes ...
Blanc M, David FPA, van der Goot FG
openaire   +3 more sources

Flotillins: At the Intersection of Protein S-Palmitoylation and Lipid-Mediated Signaling [PDF]

International Journal of Molecular Sciences, 2020
Flotillin-1 and flotillin-2 are ubiquitously expressed, membrane-associated proteins involved in multifarious cellular events from cell signaling, endocytosis, and protein trafficking to gene expression. They also contribute to oncogenic signaling.
Anna Ciesielska, Katarzyna Kwiatkowska, Orest Matveichuk   +2 more
exaly   +3 more sources

S-palmitoylation: An oily modification guardinggenome stability

DNA Repair
S-palmitoylation is a dynamic post-translational lipid modification that regulates key cellular processes. It is mediated by aspartate-histidine-histidine-cysteine-family palmitoyltransferases (PATs) and reversed by acyl-protein thioesterases (APTs).
Xiyuan, Zheng, Xinying, Wu, Lei, Wang, Haohong, Ouyang, Yeltokova, Damira, Bin, Peng, Xingzhi, Xu   +6 more
openaire   +2 more sources

S-palmitoylation modulates human estrogen receptor-α functions

Biochemical and Biophysical Research Communications, 2004
17beta-Estradiol (E2)-induced rapid functions (from seconds to minutes) can be attributed to a fraction of nuclear estrogen receptor-alpha (ERalpha) localized at the plasma membrane. As a potential mechanism, we postulated that S-palmitoylation of the Cys447 residue may explain the ability of ERalpha to associate to plasma membrane making possible E2 ...
ACCONCIA, FILIPPO, ASCENZI P., FABOZZI G., VISCA, PAOLO, MARINO, Maria   +4 more
openaire   +4 more sources

S-palmitoylation modulates estrogen receptor α localization and functions

Steroids, 2006
17beta-Estradiol (E2) acts as a chemical messenger in target tissues inducing both slow nuclear and rapid extra-nuclear responses. E2 binds to its cognate nuclear receptors (ER) resulting in the activation of target gene transcription in the nucleus.
MARINO, Maria, ASCENZI P, ACCONCIA, FILIPPO   +2 more
openaire   +5 more sources

NODs require S-palmitoylation to signal

Science, 2019
Innate Immunity The compartmentalization of proteins within the cell is essential for their function. The addition of lipid molecules redistributes proteins to the cell surface or to membrane-bound organelles. Working in transgenic mice and in tissue cultured cells, Lu et al. found that nucleotide oligomerization domain–like receptors 1 and 2 (NOD1 and
openaire   +1 more source