Results 31 to 40 of about 30,111 (219)

Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of G(i)- and G(q)-mediated signaling [PDF]

, 1999
RGS proteins (Regulators of G protein Signaling) are a recently discovered family of proteins that accelerate the GTPase activity of heterotrimeric G protein α subunits of the i, q, and 12 classes.
Backlund, Peter S., Caron, Joan M., Chen, Ching-Kang, Druey, Kirk M., Jones, Teresa L. Z., Ugur, Ozlem   +5 more
core   +1 more source

PPT1 regulation of HSP90α depalmitoylation participates in the pathogenesis of hyperandrogenism

iScience, 2023
Summary: Ovarian granulosa cells (GCs) in the follicle are the important mediator of steroidogenesis and foster oocyte maturation. Evidences suggested that the function of GCs could be regulated by S-palmitoylation.
Tongmin Xue, Shanmeizi Zhao, Hong Zhang, Ting Tang, Lu Zheng, Jun Jing, Xie Ge, Rujun Ma, Jinzhao Ma, Xiaoyan Ren, Kadiliya Jueraitetibaike, Zhigang Guo, Li Chen, Bing Yao   +13 more
doaj   +1 more source

Palmitoylation of Desmoglein 2 Is a Regulator of Assembly Dynamics and Protein Turnover. [PDF]

, 2016
Desmosomes are prominent adhesive junctions present between many epithelial cells as well as cardiomyocytes. The mechanisms controlling desmosome assembly and remodeling in epithelial and cardiac tissue are poorly understood.
Johnson, Keith R., Kowalczyk, Andrew P., Lewis, Joshua D., Mahoney, My G., Overmiller, Andrew M., Roberts, Brett J., Svoboda, Robert A., Wahl, James K.   +7 more
core   +2 more sources

Function of Protein S-Palmitoylation in Immunity and Immune-Related Diseases

Frontiers in Immunology, 2021
Protein S-palmitoylation is a covalent and reversible lipid modification that specifically targets cysteine residues within many eukaryotic proteins. In mammalian cells, the ubiquitous palmitoyltransferases (PATs) and serine hydrolases, including acyl ...
Yuqi Zhang, Ziran Qin, Wenhuan Sun, Feng Chu, Fangfang Zhou   +4 more
doaj   +1 more source

Identification of Giardia lamblia DHHC Proteins and the Role of Protein S-palmitoylation in the Encystation Process [PDF]

, 2014
Protein S-palmitoylation, a hydrophobic post-translational modification, is performed by protein acyltransferases that have a common DHHC Cys-rich domain (DHHC proteins), and provides a regulatory switch for protein membrane association. In this work, we
A Criscuolo, A Hiltpold, A Krogh, AB Hehl, AF Roth, AF Roth, AI Magee, Andrea S. Rópolo, B Eisenhaber, BC Jennings, BJ Davids, BJ Davids, BR Martin, BT Emmer, C Aicart-Ramos, C Aurrecoechea, C Faso, C Notredame, C Salaun, Cecilia V. Vranych, CH Sun, CH Sun, CH Wang, D Lloyd, DA Mitchell, DA Mitchell, DB Keister, DJ Bartels, DS Reiner, DS Reiner, EG Politis, F Abascal, FD Gillin, G DeJesus, GE Tusnady, GE Tusnady, HD Lujan, HD Lujan, HG Elmendorf, HG Morrison, I Letunic, I Letunic, I Slavin, J Greaves, J Greaves, J Greaves, J Pei, J Ren, J Schindelin, J Schultz, J Wan, J Yee, JA Duncan, JE Smotrys, JO Ebinu, JR Beck, JT Dunphy, K Frenal, KB Nicholas, KJ Livak, L Morf, LH Su, M Anisimova, M Fukata, M Punta, M Saric, María C. Merino, María C. Touz, MC Touz, MC Touz, MC Touz, MC Touz, MD Resh, ME Linder, ME Linder, MG De Napoli, ML Jones, ML Jones, MM Corvi, MM Zhang, MR Rivero, MS Brown, N Gottig, Nahuel Zamponi, O Batistic, O Rocks, P Papanastasiou, PG Carranza, R Tsutsumi, RD Adam, RD Finn, S Guindon, S Lobo, S Sonda, S Stoven, SE Boucher, SF Chuang, SL Planey, SM Singer, SR Birkeland, Steven M. Singer, T Hoppe, T Lauwaet, TE Nash, TE Nash, TN Petersen, TS Worgall, WF Leong, Y Fukata, Y He, Y Huang, Y Ohno, Y Webb, YC Huang, YJ Pan   +114 more
core   +3 more sources

Palmitoylated proteins in Ureaplasma urealyticum [PDF]

Infection and Immunity, 1991
After incubation of Ureaplasma urealyticum serotype 8 in the presence of 3H-labeled palmitic acid, about 25 acylated proteins were detected by electrophoresis and fluorography. Of these, at least six were shown to be antigenic by immunoprecipitation of solubilized palmitate-labeled cells with a homologous polyclonal serum.
D, Thirkell, A D, Myles, W C, Russell
openaire   +2 more sources

ATP-independent Control of Vac8 Palmitoylation by a SNARE Subcomplex on Yeast Vacuoles [PDF]

, 2005
Yeast vacuole fusion requires palmitoylated Vac8. We previously showed that Vac8 acylation occurs early in the fusion reaction, is blocked by antibodies against Sec18 (yeast N-ethylmaleimide-sensitive fusion protein (NSF)), and is mediated by the R-SNARE
Cristodero, Marina, Dietrich, Lars E. P., LaGrassa, Tracy J., Meiringer, Christoph T. A., Rohde, Jan, Ungermann, Christian   +5 more
core   +1 more source

Acid Sphingomyelinase Regulates the Localization and Trafficking of Palmitoylated Proteins [PDF]

, 2019
In human, loss of Acid Sphingomeylinase (ASM/SMPD1) causes Niemann-Pick Disease, type A. ASM hydrolyzes sphingomyelins to produce ceramides but protein targets of ASM remain largely unclear. ...
Kim, Yongsoon, Lee, Chia-Fang, Li, Wenjing, Sun, Hong, Xiong, Xiahui, Yu, Jiekai, Zhang, Hul, Zhu, Linyu   +7 more
core   +2 more sources

Quantifying protein densities on cell membranes using super-resolution optical fluctuation imaging [PDF]

, 2017
Surface molecules, distributed in diverse patterns and clusters on cell membranes, influence vital functions of living cells. It is therefore important to understand their molecular surface organisation under different physiological and pathological ...
Benda, Aleš, Brdička, Tomáš, Cebecauer, Marek, Glatzová, Daniela, Kvíčalová, Zuzana, Lasser, Theo, Letschert, Sebastian, Levet, Florian, Lukeš, Tomáš, Sauer, Markus   +9 more
core   +11 more sources

Posttranslational modifications of GLUT4 affect its subcellular localization and translocation [PDF]

, 2013
The facilitative glucose transporter type 4 (GLUT4) is expressed in adipose and muscle and plays a vital role in whole body glucose homeostasis. In the absence of insulin, only ~1% of cellular GLUT4 is present at the plasma membrane, with the vast ...
Bayer, Begum, Birnbaum, Bogan, Bogan, Bogan, Bryant, Cassie Welburn, Chang, Fujita, Garvey, Gill, Giorgino, Govers, Grasbon-Frodl, Gwyn Gould, Haga, Hardy, Herrmann, Hicke, Huang, Ing, James, James, Jessica Sadler, Jeyaraj, Karylowski, Kupriyanova, Lamb, Lau, Lawrence, Lawrence, Leto, Li, Liu, Livingstone, Mahajan, Marsh, Marshall, Marshall, Martin, Matunis, McCormick, Muller, Nia Bryant, Perera, Pessin, Pilch, Piper, Ren, Reusch, Saltiel, Semiz, Shi, Shi, Stöckli, Toh, Urbe, Vannucci, Varki, Watson, Williams, Yang, Yu, Zaarour   +64 more
core   +3 more sources