PalmS-ESRs:CAVs translocate to plasma membrane

Stable Identifier
Reaction [omitted]
Homo sapiens
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Palmitoylation of estrogen receptors promotes their interaction with caveolin (CAV), which is required for their translocation to the plasma membrane where they function in rapid, transcription-independent signaling (Chambliss et al, 2002; Razandi et al, 2003; Acconcia et al, 2004; Pedram et al, 2007; Razandi et al, 2010; Pedram et al, 2012; reviewed in Schwartz et al, 2016). Approximately 5-15% of total cellular estrogen receptor is at the plasma membrane where it is enriched in caveolae (Pedram et al, 2006; Marino et al, 2006).

Literature References
PubMed ID Title Journal Year
15033483 S-palmitoylation modulates human estrogen receptor-alpha functions

Acconcia, F, Ascenzi, P, Fabozzi, G, Visca, P, Marino, M

Biochem. Biophys. Res. Commun. 2004
11981029 ERbeta has nongenomic action in caveolae

Chambliss, KL, Yuhanna, IS, Anderson, RG, Mendelsohn, ME, Shaul, PW

Mol. Endocrinol. 2002
12588983 Identification of a structural determinant necessary for the localization and function of estrogen receptor alpha at the plasma membrane

Razandi, M, Alton, G, Pedram, A, Ghonshani, S, Webb, P, Levin, ER

Mol. Cell. Biol. 2003
17535799 A conserved mechanism for steroid receptor translocation to the plasma membrane

Pedram, A, Razandi, M, Sainson, RC, Kim, JK, Hughes, CC, Levin, ER

J. Biol. Chem. 2007
16274718 S-palmitoylation modulates estrogen receptor alpha localization and functions

Marino, M, Ascenzi, P, Acconcia, F

Steroids 2006
22031296 DHHC-7 and -21 are palmitoylacyltransferases for sex steroid receptors

Pedram, A, Razandi, M, Deschenes, RJ, Levin, ER

Mol. Biol. Cell 2012
16645038 Nature of functional estrogen receptors at the plasma membrane

Pedram, A, Razandi, M, Levin, ER

Mol. Endocrinol. 2006
20439495 Heat shock protein 27 is required for sex steroid receptor trafficking to and functioning at the plasma membrane

Razandi, M, Pedram, A, Levin, ER

Mol. Cell. Biol. 2010
27288742 Rapid steroid hormone actions via membrane receptors

Schwartz, N, Verma, A, Bivens, CB, Schwartz, Z, Boyan, BD

Biochim. Biophys. Acta 2016
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