S-palmitoylation modulates human estrogen receptor-α functions

Acconcia, Filippo; Ascenzi, Paolo; Fabozzi, Giulia; Visca, Paolo; Marino, Maria

doi:10.1016/j.bbrc.2004.02.129

Cited by 156 publications

(117 citation statements)

References 33 publications

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“…In recent years, a large number of reports have described membrane-associated estrogen receptors, either similar to or distinct from the classical nuclear estrogen receptors (Acconcia et al, 2004;Li et al, 2003;Razandi et al, 2003;Toran-Allerand et al, 2002). These receptors have been postulated to mediate aspects of cellular estrogen function, including traditional genomic (transcriptional) signaling as well as novel nongenomic (rapid) signaling (Govind and Thampan, 2003).…”

Section: Membrane-associated Estrogen Receptorsmentioning

confidence: 99%

“…These non-genomic signaling events include pathways that are traditionally thought of as arising from transmembrane growth factor receptors and G protein-coupled receptors. Whereas some reports described estrogen binding sites on intracellular membranes (Evans and Muldoon, 1991), other reports suggest that palmitoylation (Acconcia et al, 2004;Li et al, 2003) or phosphorylation (Balasenthil et al, 2004;Wang et al, 2002) may target classical ERs to the cytoplasmic face of the plasma membrane. Additional reports have suggested the involvement of adaptor proteins, such as Shc (Evinger and Levin, 2005) and MNAR (Boonyaratanakornkit and Edwards, 2004), in the recruitment of ERα to the plasma membrane and caveolae in particular.…”

Section: Membrane-associated Estrogen Receptorsmentioning

confidence: 99%

“…PI 3-kinase, Akt, MAPK family members, Src family members, and PKA/PKC) (Hall et al, 2001;Ho and Liao, 2002;Kelly and Levin, 2001;Levin, 2001;Levin, 2002;Razandi et al, 2003). In many reports, the estrogen-responsive receptor is proposed to be ER itself (either α or β), or a modified form of the protein (Acconcia et al, 2004;Li et al, 2003). Complexes between the classical ERs and G proteins (Navarro et al, 2003) as well as with PI3 kinase (Simoncini et al, 2003) have been described.…”

Section: Estrogen-mediated Non-genomic Signalingmentioning

confidence: 99%

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GPR30: A G protein-coupled receptor for estrogen

Prossnitz

Arterburn

Sklar

2007

Molecular and Cellular Endocrinology

272

186

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Estrogen is a critical steroid in human physiology exerting its effect both at the transcriptional level as well as at the level of rapid intracellular signaling through second messengers. Many of estrogen's transcriptional effects have long been known to be mediated through classical nuclear steroid receptors but recent studies also demonstrate the existence of a 7-transmembrane G protein-coupled receptor, GPR30 that responds to estrogen with rapid cellular signaling. There is currently controversy over the ability of classical estrogen receptors to recapitulate GPR30-mediated signaling mechanisms and vice versa. This article will summarize recent literature and address the relationship between GPR30 and conventional estrogen receptor signaling.

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Section: Membrane-associated Estrogen Receptorsmentioning

confidence: 99%

Section: Membrane-associated Estrogen Receptorsmentioning

confidence: 99%

Section: Estrogen-mediated Non-genomic Signalingmentioning

confidence: 99%

See 1 more Smart Citation

GPR30: A G protein-coupled receptor for estrogen

Prossnitz

Arterburn

Sklar

2007

Molecular and Cellular Endocrinology

272

186

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“…Although research has focused primarily on palmitoylation of ERα and its variants [64,[67][68][69], the same mechanism for caveolae association has been described for ERβ [64,70]. Specifically, palmitoylation of human ERα at cysteine 447 (mouse 451) is essential for receptor interaction with CAV1 and its subsequent localization to the plasma membrane.…”

Section: Caveolin Proteins and Estrogen Receptorsmentioning

confidence: 99%

Caveolin proteins and estrogen signaling in the brain

Luoma

Boulware

Mermelstein

2008

Molecular and Cellular Endocrinology

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Best described outside the nervous system, caveolins are structural proteins that form caveolae, functional microdomains at the plasma membrane that cluster related signaling molecules. Caveolin associated proteins include G protein coupled receptors and G proteins, receptor tyrosine kinases, as well as protein kinases, ion channels and various other signaling enzymes. Not surprisingly, a wide array of biological disorders are thought to be rooted in caveolin dysfunction. In addition, caveolins also traffic and cluster estrogen receptors to caveolae. Interactions between the estrogen receptors ERα and ERβ with caveolins appear critical in many non-neuronal cell types, e.g. disruption of normal function may underlie many forms of breast cancer. Recent findings suggest caveolins may also play an essential role in membrane estrogen receptor function in the nervous system. Not only are they expressed in neurons and glia, but different caveolin isoforms also appear necessary to generate distinct functional signaling complexes. With membrane estrogen receptors responsible for the efficient activation of a multitude of intracellular signaling pathways, which in turn influence a wide variety of nervous system functions, caveolin proteins are poised to act as the central coordinators of these processes.

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“…Le fractionnement des membranes plasmiques de cellules endothéliales a révélé une association de ER extranucléaire avec en particulier, mais pas exclusivement, des cavéoles dans lesquelles le récepteur participe à une véritable plateforme de signalisation [20] ( Figure 3). Une fraction d'ER est en effet adressée à la membrane cytoplasmique grâce à la palmitoylation de la cystéine 447 qui permet son interaction avec la cavéoline-1 [27,28] (Figure 3 extranucléaire induite par ER [32]. Outre l'activation de la eNOS au niveau de l'endothélium, des effets membranaires du récepteur ont également été décrits dans de nombreux autres types cellulaires.…”

Section: Erα36unclassified