ArticleThe Journal of biological chemistry2012
Identification of a novel LXXLL motif in α-actinin 4-spliced isoform that is critical for its interaction with estrogen receptor α and co-activators.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 29 citations in OpenAlex.
- Review
- Article
- Protein tyrosine phosphatase 1B is a regulator of alpha-actinin4 in the glomerular podocyte.Biochimica et biophysica acta. Molecular cell research · 2024Article
- Cytochrome-c-oxidase and ATPsynthase content increases in the endometrium of the patients with adenomyosis.Molecular biology reports · 2023Article
- Article
- CLPTM1L induces estrogen receptor β signaling-mediated radioresistance in non-small cell lung cancer cells.Cell communication and signaling : CCS · 2020Article
- Kidney podocyte-associated gene polymorphisms affect tacrolimus concentration in pediatric patients with refractory nephrotic syndrome.The pharmacogenomics journal · 2020Article
- Review
- Article
- Candidate biomarkers in the cervical vaginal fluid for the (self-)diagnosis of cervical precancer.Archives of gynecology and obstetrics · 2018Review
- α Actinin 4 (ACTN4) Regulates Glucocorticoid Receptor-mediated Transactivation and Transrepression in Podocytes.The Journal of biological chemistry · 2017Article
- Pathway analysis supports association of nonsyndromic cryptorchidism with genetic loci linked to cytoskeleton-dependent functions.Human reproduction (Oxford, England) · 2015Article
- Alpha actinin-1 regulates cell-matrix adhesion organization in keratinocytes: consequences for skin cell motility.The Journal of investigative dermatology · 2015Article
- α-Actinin 4 potentiates nuclear factor κ-light-chain-enhancer of activated B-cell (NF-κB) activity in podocytes independent of its cytoplasmic actin binding function.The Journal of biological chemistry · 2015Article
- The biological role of actinin-4 (ACTN4) in malignant phenotypes of cancer.Cell & bioscience · 2015Article
- The role of alpha-actinin-4 in human kidney disease.Cell & bioscience · 2015Article
- The actinin family of actin cross-linking proteins - a genetic perspective.Cell & bioscience · 2015Article
- The actinin family proteins: biological function and clinical implications.Cell & bioscience · 2015Article
- Small leucine zipper protein (sLZIP) negatively regulates skeletal muscle differentiation via interaction with α-actinin-4.The Journal of biological chemistry · 2014Article
- Identification of protein biomarkers for cervical cancer using human cervicovaginal fluid.PloS one · 2014Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
α-Actinins (ACTNs) are a family of proteins cross-linking actin filaments that maintain cytoskeletal organization and cell motility. Recently, it has also become clear that ACTN4 can function in the nucleus. In this report, we found that ACTN4 (full length) and its spliced isoform ACTN4 (Iso) possess an unusual LXXLL nuclear receptor interacting motif. Both ACTN4 (full length) and ACTN4 (Iso) potentiate basal transcription activity and directly interact with estrogen receptor α, although ACTN4 (Iso) binds ERα more strongly. We have also found that both ACTN4 (full length) and ACTN4 (Iso) interact with the ligand-independent and the ligand-dependent activation domains of estrogen receptor α. Although ACTN4 (Iso) interacts efficiently with transcriptional co-activators such as p300/CBP-associated factor (PCAF) and steroid receptor co-activator 1 (SRC-1), the full length ACTN4 protein either does not or does so weakly. More importantly, the flanking sequences of the LXXLL motif are important not only for interacting with nuclear receptors but also for the association with co-activators. Taken together, we have identified a novel extended LXXLL motif that is critical for interactions with both receptors and co-activators. This motif functions more efficiently in a spliced isoform of ACTN4 than it does in the full-length protein.
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Registered trials
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.