Lipid raft localization and palmitoylation: Identification of two requirements for cell death induction by the tumor suppressors UNC5H

Maisse, Carine; Rossin, Aurélie; Cahuzac, Nathalie; Paradisi, Andrea; Klein, C; Haillot, Marie-Laure; Hérincs, Zoltán; Mehlen, Patrick; Hueber, Anne-Odile

doi:10.1016/j.yexcr.2008.06.001

Cited by 19 publications

(19 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Net accumulation of immune cells in aortic plaques is proportional to monocyte recruitment from bone marrow along with peripheral proliferation, including within the plaque, that is counterbalanced by the emigration and death of macrophages. A new focus on this process has examined how cholesterol loading of macrophages increased the expression of netrin 1 and semaphorin 3E, which inhibit migration causing retention of macrophages in atherosclerotic lesions, a process that involves lipid raft microdomains where both receptors are located . Activation and proliferation of immune cells drives atherosclerosis and is characterized in hypercholesterolemic animal models by a sharp increase in the number of Ly‐6C hi monocytes in circulation that are recruited to plaques .…”

Section: Discussionmentioning

confidence: 99%

“…A new focus on this process 57,89 has examined how cholesterol loading of macrophages increased the expression of netrin 1 and semaphorin 3E, which inhibit migration causing retention of macrophages in atherosclerotic lesions, [90][91][92] a process that involves lipid raft microdomains where both receptors are located. [92][93][94][95] Activation and proliferation of immune cells drives atherosclerosis and is characterized in hypercholesterolemic animal models by a sharp increase in the number of Ly-6C hi monocytes in circulation that are recruited to plaques. 54,55,96 Cholesterol accumulation by monocytes significantly affects the recruitment and proliferation of these inflammatory monocytes.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Lipid‐Free Apolipoprotein A‐I Reduces Progression of Atherosclerosis by Mobilizing Microdomain Cholesterol and Attenuating the Number of CD131 Expressing Cells: Monitoring Cholesterol Homeostasis Using the Cellular Ester to Total Cholesterol Ratio

Kaul

Zabalawi

et al. 2016

JAHA

View full text Add to dashboard Cite

BackgroundAtherosclerosis is a chronic inflammatory disorder whose development is inversely correlated with high‐density lipoprotein concentration. Current therapies involve pharmaceuticals that significantly elevate plasma high‐density lipoprotein cholesterol concentrations. Our studies were conducted to investigate the effects of low‐dose lipid‐free apolipoprotein A‐I (apoA‐I) on chronic inflammation. The aims of these studies were to determine how subcutaneously injected lipid‐free apoA‐I reduces accumulation of lipid and immune cells within the aortic root of hypercholesterolemic mice without sustained elevations in plasma high‐density lipoprotein cholesterol concentrations.Methods and Results Ldlr −/− and Ldlr −/− apoA‐I −/− mice were fed a Western diet for a total of 12 weeks. After 6 weeks, a subset of mice from each group received subcutaneous injections of 200 μg of lipid‐free human apoA‐I 3 times a week, while the other subset received 200 μg of albumin, as a control. Mice treated with lipid‐free apoA‐I showed a decrease in cholesterol deposition and immune cell retention in the aortic root compared with albumin‐treated mice, regardless of genotype. This reduction in atherosclerosis appeared to be directly related to a decrease in the number of CD131 expressing cells and the esterified cholesterol to total cholesterol content in several immune cell compartments. In addition, apoA‐I treatment altered microdomain cholesterol composition that shifted CD131, the common β subunit of the interleukin 3 receptor, from lipid raft to nonraft fractions of the plasma membrane.ConclusionsApoA‐I treatment reduced lipid and immune cell accumulation within the aortic root by systemically reducing microdomain cholesterol content in immune cells. These data suggest that lipid‐free apoA‐I mediates beneficial effects through attenuation of immune cell lipid raft cholesterol content, which affects numerous types of signal transduction pathways that rely on microdomain integrity for assembly and activation.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Lipid‐Free Apolipoprotein A‐I Reduces Progression of Atherosclerosis by Mobilizing Microdomain Cholesterol and Attenuating the Number of CD131 Expressing Cells: Monitoring Cholesterol Homeostasis Using the Cellular Ester to Total Cholesterol Ratio

Kaul

Zabalawi

et al. 2016

JAHA

View full text Add to dashboard Cite

show abstract

“…S-acylation of the neurotensin receptor 1 (NTSR-1), a key mediator in breast, pancreas, prostate, colon and lung cancers, is essential for its localization and efficient signaling (Heakal et al, 2011). The induction of apoptosis is an efficient way to stop tumor development, many proteins involved in apoptosis are S-acylated including FasL (Fas Ligand; Guardiola-Serrano et al, 2010), FasR (Fas receptor; Chakrabandhu et al, 2007), DR4 (a receptor of the tumor necrosis factor-related apoptosis-inducing ligand; Rossin et al, 2009), DCC (deleted in colorectal cancer; Furne et al, 2006), UNC5H (Maisse et al, 2008) and BAX (BCL-2-associated X) (Fröhlich et al, 2014). The spread of cancer cells from their original site to other parts of the body is through metastasis.…”

Section: S-acylationmentioning

confidence: 99%

Progress toward Understanding Protein S-acylation: Prospective in Plants

2017

Front. Plant Sci.

View full text Add to dashboard Cite

S-acylation, also known as S-palmitoylation or palmitoylation, is a reversible post-translational lipid modification in which long chain fatty acid, usually the 16-carbon palmitate, covalently attaches to a cysteine residue(s) throughout the protein via a thioester bond. It is involved in an array of important biological processes during growth and development, reproduction and stress responses in plant. S-acylation is a ubiquitous mechanism in eukaryotes catalyzed by a family of enzymes called Protein S-Acyl Transferases (PATs). Since the discovery of the first PAT in yeast in 2002 research in S-acylation has accelerated in the mammalian system and followed by in plant. However, it is still a difficult field to study due to the large number of PATs and even larger number of putative S-acylated substrate proteins they modify in each genome. This is coupled with drawbacks in the techniques used to study S-acylation, leading to the slower progress in this field compared to protein phosphorylation, for example. In this review we will summarize the discoveries made so far based on knowledge learnt from the characterization of protein S-acyltransferases and the S-acylated proteins, the interaction mechanisms between PAT and its specific substrate protein(s) in yeast and mammals. Research in protein S-acylation and PATs in plants will also be covered although this area is currently less well studied in yeast and mammalian systems.

show abstract

“…DAPK can also form heterocomplexes composed of HSP90 and CHIP or DIP1/Mib1, indicating that the heightened surveillance and modulation of DAPK activities is critical to accurate regulation of apoptosis and cellular homeostasis (Zhang et al, 2007). An interaction between UNC5C (UNC5H3) and DAPK1 was demonstrated (Llambi et al, 2005), whereby this interaction was shown to be dependent on both UNC5H2 lipid raft localization and palmitoylation (Maisse et al, 2008). An interaction between DAPK1 promoter and transcription factors ATF2 and c-jun was demons-trated in cisplatin-treated human breast cancer cells (Hayakawa et al, 2004).…”

Section: Interaction Partnersmentioning

confidence: 99%