Valeria Pesiri
PhosphorylationUbiquitin ligaseEstrogen receptor alphaChemistryEstrogen-related receptor alphaUbiquitinMonoubiquitinationCancer researchBiochemistryCell growthSignal transductionProtein kinase BEndocytic cycleIntracellularEstrogen receptorTranscription factorPI3K/AKT/mTOR pathwayBiologyCell biologyEstrogen receptor beta
12Publications
7H-index
191Citations
Publications 12
Newest
#1Valeria PesiriH-Index: 7
#2Elena Di MuzioH-Index: 5
Last. Filippo AcconciaH-Index: 30
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Ubiquitin (Ub)-binding domains (UBDs) noncovalently contact the Ub modification on binding partners. Ub possesses seven lysine (K) residues (i.e., K6, K11, K27, K29, K33, K48, and K63) that can be used to form different chains based on different Ub linkage types (e.g., monoubiquitination/polyubiquitination). Thus, different Ub-based signals exist and are decoded by UBDs. Recently, we have reported the existence of two Ub binding surfaces located within the estrogen receptor α (ERα) protein. We h...
5 CitationsSource
#1Valeria PesiriH-Index: 7
#2Pierangela TottaH-Index: 16
Last. Filippo AcconciaH-Index: 30
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Abstract 17β-Estradiol (E2)-dependent cell proliferation requires both estrogen receptor α (ERα)-based integrated control of gene transcription and kinase pathways activation. Such coordination of intracellular E2:ERα-dependent signaling mechanisms is finely tuned by receptor association with specific partner proteins. Recently, we identified the leucine (L) 429 and alanine (A) 430 within the ERα ligand binding domain as important residues for receptor non-covalent interaction to ubiquitinated s...
13 CitationsSource
#1Pierangela TottaH-Index: 16
#2Valeria PesiriH-Index: 7
Last. Filippo AcconciaH-Index: 30
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17β-estradiol (E2)-induced signaling and control of estrogen receptor (ER)α degradation both play a major role in breast cancer cell proliferation. We recently reported the involvement of lysosomal function in both E2-dependent ERα breakdown and E2-induced cell proliferation and thus hypothesized a role for endocytic proteins in ERα signaling. An small interfering RNA screen identified proteins that regulate intracellular endocytic traffic and whose silencing alters E2-induced ERα degradation. O...
15 CitationsSource
1 CitationsSource
#1Valeria PesiriH-Index: 7
#2Pierangela TottaH-Index: 16
Last. Filippo AcconciaH-Index: 30
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The sex steroid hormone 17β-estradiol (E2) regulates breast cancer (BC) cell proliferation and migration through the activation of a plethora of signal transduction cascades (e.g., PI3K/AKT activation) starting after E2 binding to the estrogen receptor alpha (ERα). The activity of the ubiquitin (Ub)-system modulates many physiological processes (e.g., cell proliferation and migration), and recently, a specific inhibitor (Pyr-41) of the Ub-activating enzyme (E1), which works as the activator of t...
9 CitationsSource
#1Pierangela TottaH-Index: 16
#2Valeria PesiriH-Index: 7
Last. Filippo AcconciaH-Index: 30
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The homeostatic control of the cellular proteome steady-state is dependent either on the 26S proteasome activity or on the lysosome function. The sex hormone 17β-estradiol (E2) controls a plethora of biological functions by binding to the estrogen receptor α (ERα), which is both a nuclear ligand-activated transcription factor and also an extrinsic plasma membrane receptor. Regulation of E2-induced physiological functions (e.g., cell proliferation) requires the synergistic activation of both tran...
27 CitationsSource
#1Valeria PesiriH-Index: 7
#2Piergiorgio La RosaH-Index: 13
Last. Filippo AcconciaH-Index: 30
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Summary Ubiquitin (Ub)-binding domains (UBDs) located in Ub receptors decode the ubiquitination signal by non-covalently engaging the Ub modification on their binding partners and transduce the Ub signalling through Ub-based molecular interactions. In this way, inducible protein ubiquitination regulates diverse biological processes. The estrogen receptor alpha (ERα) is a ligand-activated transcription factor that mediates the pleiotropic effects of the sex hormone 17β-estradiol (E2). Fine regula...
13 CitationsSource
#2Valeria PesiriH-Index: 7
Last. Filippo AcconciaH-Index: 3
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#1Valeria PesiriH-Index: 7
#2Filippo AcconciaH-Index: 3
Source
#1Piergiorgio La RosaH-Index: 13
#1Piergiorgio La Rosa (Roma Tre University)H-Index: 2
Last. Filippo AcconciaH-Index: 30
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The estrogen receptor-α (ERα) is a transcription factor that regulates gene expression through the binding to its cognate hormone 17β-estradiol (E2). ERα transcriptional activity is regulated by E2-evoked 26S proteasome-mediated ERα degradation and ERα serine (S) residue 118 phosphorylation. Furthermore, ERα mediates fast cell responses to E2 through the activation of signaling cascades such as the MAPK/ERK and phosphoinositide-3-kinase/v-akt murine thymoma viral oncogene homolog 1 pathways. The...
83 CitationsSource
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