Calmodulin-independent, agonistic properties of a peptide containing the calmodulin binding site of estrogen receptor α

Gallo, Dominique; Jacquemotte, F; Cleeren, Anny; Laı̈os, Ioanna; Hadiy, Samira; Rowlands, Martin; Caille, Olivier; Nonclercq, Denis; Laurent, Guy; Jacquot, Yves; Leclercq, Guy

doi:10.1016/j.mce.2007.01.012

Cited by 32 publications

(69 citation statements)

References 54 publications

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“…reported to generate high basal, E 2 -independent transcription of reporter genes (Gallo et al, 2007a;Li et al, 2005). From this finding one may surmise that the D/E border region to which CaM binds stabilizes the receptor in an inactive status.…”

Section: Mutations (Deletions/substitutions) Of Erα Affecting Cam Binmentioning

confidence: 75%

“…Page 7 (P 295 LMIKRSKKNSLALSTADQMVS 317 ), thus at the boundary between the hinge and the ligand binding domain (Gallo et al, 2007a;Li et al, 2005). Although the contribution of most of these aminoacid residues in terms of interaction with CaM is unknown, the importance of Ile-298, and Lys-299, 302 and 303 must, however, be stressed.…”

Section: A Cam Binding Domain Has Been Localized In Erαmentioning

confidence: 99%

“…To explore further ERα interaction with CaM, we synthesized a peptide containing these major determinants (ERα17p : P 295 -T 311 ), as well as two control peptides in which Lys-302 and 303 were substituted by alanines (ERα17pAA) or glycines (ERα17pGG) (Gallo et al, 2007a ERα-CaM association (see # 8).…”

Section: A Cam Binding Domain Has Been Localized In Erαmentioning

confidence: 99%

“…ERα down regulation, induction of pS2 and progesterone receptor, growth stimulation…) (Gallo et al, 2007a;Gallo et al, 2007b;Gallo et al, 2008a). Assessment of a panel of breast cancer cell lines revealed that the trophic effect of these peptides was restricted to ERα-positive cell lines, establishing the implication of the receptor in their biological effect.…”

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confidence: 99%

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Calmodulin, a regulatory partner of the estrogen receptor alpha in breast cancer cells

Gallo

Jacquot²,

Laurent

et al. 2008

Molecular and Cellular Endocrinology

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Section: Mutations (Deletions/substitutions) Of Erα Affecting Cam Binmentioning

confidence: 75%

Section: A Cam Binding Domain Has Been Localized In Erαmentioning

confidence: 99%

Section: A Cam Binding Domain Has Been Localized In Erαmentioning

confidence: 99%

mentioning

confidence: 99%

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Calmodulin, a regulatory partner of the estrogen receptor alpha in breast cancer cells

Gallo

Jacquot²,

Laurent

et al. 2008

Molecular and Cellular Endocrinology

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“…This 17 amino acid motif of ER is responsible for a number of posttranscriptional modifications as well as of the recruitment of co-regulators. It was reported to elicit (pseudo)-estrogenic responses in ER+ MCF-7 cells (Gallo et al, 2007). Further studies showed that the ER 17p peptide induced apoptosis in the ER+ MCF-7 and T47D cells and also in the ER-MDA-MB-231 and SKBr-3 cells through ER independent mechanisms.…”

Section: Introductionmentioning

confidence: 96%

Metabolomics and Transcriptional Responses in Estrogen Receptor Positive Breast Cancer Cells

Mandal¹,

Khan²,

Li³

et al. 2011

Breast Cancer - Carcinogenesis, Cell Growth and Signalling Pathways

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ERα17p, an ERα P295-T311 fragment, modifies the migration of breast cancer cells, through actin cytoskeleton rearrangements

et al. 2011

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Recently, our knowledge on estrogen receptor alpha (ERα) functions and fate has progressed: ERα enters in repeated transcription-modulating cycles (nucleus/cytoplasm/membrane trafficking processes and proteasomal degradation) that are governed by specific protein-protein interactions. Receptor fragments, especially those resulting from the proteolysis of its ligand binding domain, as well as corresponding synthetic peptides, have been studied with respect to their estrogenic/antiestrogenic potency. A peptide, corresponding to the human ERα P(295) -T(311) sequence (ERα17p) has been shown to alter breast cancer cell fate, triggering proliferation, or apoptosis. The aim of this work was to explore the effect of ERα17p on breast cancer cell migration and actin cytoskeleton dynamics and further analyze the mechanism of its membrane action. We show that ERα17p increases (MCF-7 and SK-BR-3 cells) or decreases (T47D and MDA-MB-231 cells) migration of breast cancer cells, in an ERα-independent manner, by mechanism(s) depending on Rho/ROCK and PI3K/Akt signaling pathways. Moreover, the peptide enhances the association of both estrogens and androgens to membranes and modifies cell migration, induced by E(2) -BSA. Additionally, initial evidence of a possible agonistic action of the peptide on GPR30 is also provided. ERα17p can be considered as a cell migration-modulator and could therefore constitute a therapeutic challenge, even in anti-estrogen-resistant tumors.

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Calmodulin-independent, agonistic properties of a peptide containing the calmodulin binding site of estrogen receptor α

Cited by 32 publications

References 54 publications

Calmodulin, a regulatory partner of the estrogen receptor alpha in breast cancer cells

Calmodulin, a regulatory partner of the estrogen receptor alpha in breast cancer cells

Metabolomics and Transcriptional Responses in Estrogen Receptor Positive Breast Cancer Cells

ERα17p, an ERα P295-T311 fragment, modifies the migration of breast cancer cells, through actin cytoskeleton rearrangements

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