ArticleMolecular and cellular biology2007
Specific amino acid residues in the basic helix-loop-helix domain of SRC-3 are essential for its nuclear localization and proteasome-dependent turnover.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 45 citations in OpenAlex.
- Nuclear receptor coregulator interactions: beyond the switch.Genes & development · 2026Review
- Transcriptional Cofactors for Thyroid Hormone Receptors.Endocrinology · 2025Review
- Functional Characterization of an In-Frame Deletion in the Basic Domain of the Retinal Transcription Factor ATOH7.International journal of molecular sciences · 2022Article
- Targeting the NCOA3-SP1-TERT axis for tumor growth in hepatocellular carcinoma.Cell death & disease · 2020Article
- Phosphorylation of steroid receptor coactivator-3 (SRC-3) at serine 857 is regulated by the p38Scientific reports · 2020Article
- The F-box protein FBXL16 up-regulates the stability of C-MYC oncoprotein by antagonizing the activity of the F-box protein FBW7.The Journal of biological chemistry · 2020Article
- Minireview: nuclear receptor coregulators of the p160 family: insights into inflammation and metabolism.Molecular endocrinology (Baltimore, Md.) · 2015Review
- Steroid receptor coactivator 1 is an integrator of glucose and NAD+/NADH homeostasis.Molecular endocrinology (Baltimore, Md.) · 2014Article
- Nuclear receptor coactivators: master regulators of human health and disease.Annual review of medicine · 2014Review
- The nuclear cofactor RAC3/AIB1/SRC-3 enhances Nrf2 signaling by interacting with transactivation domains.Oncogene · 2013Article
- Nuclear receptor coactivator RAC3 inhibits autophagy.Cancer science · 2012Article
- Steroid receptor coactivator-3 as a potential molecular target for cancer therapy.Expert opinion on therapeutic targets · 2012Review
- Glucocorticoid-dependent phosphorylation of the transcriptional coregulator GRIP1.Molecular and cellular biology · 2012Article
- Steroid receptor coactivators 1, 2, and 3: critical regulators of nuclear receptor activity and steroid receptor modulator (SRM)-based cancer therapy.Molecular and cellular endocrinology · 2012Review
- The function of steroid receptor coactivator-1 in normal tissues and cancer.International journal of biological sciences · 2012Review
- Tumor-suppressor role for the SPOP ubiquitin ligase in signal-dependent proteolysis of the oncogenic co-activator SRC-3/AIB1.Oncogene · 2011Article
- Role of the nuclear receptor coactivator AIB1-Delta4 splice variant in the control of gene transcription.The Journal of biological chemistry · 2011Article
- Ligand-dependent degradation of SRC-1 is pivotal for progesterone receptor transcriptional activity.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Minireview: steroid receptor coactivator-3: a multifarious coregulator in mammary gland metastasis.Endocrinology · 2011Review
- Steroid receptor coactivator (SRC) family: masters of systems biology.The Journal of biological chemistry · 2010Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SRC-3/AIB1/ACTR/pCIP/RAC3/TRAM-1 is a primary transcriptional coactivator for the estrogen receptor. Here we report that deletion of the SRC-3 basic helix-loop-helix (bHLH) domain blocks its proteasome-dependent turnover. We further identified two residues (K17 and R18) in the SRC-3 bHLH domain that are essential for its stability. Moreover, we found that the bHLH domain contains a bipartite nuclear localization signal (NLS). SRC-3 NLS mutants block its translocation into the nucleus, and this correlates with its insensitivity to proteasome-dependent turnover. SRC-3 shows a time-dependent decay in the presence of cycloheximide which is not apparent for the cytoplasmic mutant. Fusion of a simian virus 40 T antigen NLS to the cytoplasmic localized SRC-3 mutant drives it back into the nucleus and restores its proteasomal sensitivity. In addition, the cytoplasmic mutants are inactive for transcriptional coactivation and cancer cell growth. Taken together, our data indicate that proteasome-dependent turnover of SRC-3 occurs in the nucleus and that two amino acid residues in the bHLH domain provide a signal for its nuclear localization and proteasome-dependent degradation as well as for regulation of SRC-3 transcriptional coactivator capacity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.