ArticleThe Journal of biological chemistry2012
Protein inhibitor of activated STAT3 (PIAS3) protein promotes SUMOylation and nuclear sequestration of the intracellular domain of ErbB4 protein.
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 28 papers.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- SUMOylation of EphB4 enhances its stability in prostate cancer.British journal of cancer · 2026Article
- Disruption of the reciprocal inhibitory relationship between cell proliferation and melanogenesis in pet murine melanoma cells by ultraviolet radiation.Frontiers in veterinary science · 2026Article
- Article
- PIAS family in cancer: from basic mechanisms to clinical applications.Frontiers in oncology · 2024Review
- SUMO-activated target traps (SATTs) enable the identification of a comprehensive E3-specific SUMO proteome.Science advances · 2023Article
- Review
- STAT5b is a key effector of NRG-1/ERBB4-mediated myocardial growth.EMBO reports · 2023Article
- An extracellular receptor tyrosine kinase motif orchestrating intracellular STAT activation.Nature communications · 2022Article
- Trophic factor BDNF inhibits GABAergic signaling by facilitating dendritic enrichment of SUMO E3 ligase PIAS3 and altering gephyrin scaffold.The Journal of biological chemistry · 2022Article
- Article
- Review
- The guanine nucleotide exchange factor VAV3 participates in ERBB4-mediated cancer cell migration.The Journal of biological chemistry · 2020Article
- The multifaceted role of kinases in amyotrophic lateral sclerosis: genetic, pathological and therapeutic implications.Brain : a journal of neurology · 2020Review
- Identification of protein inhibitor of activated STAT 4, a novel host interacting partner that involved in bovine viral diarrhea virus growth.Virology journal · 2020Article
- STAT3 and STAT5 Activation in Solid Cancers.Cancers · 2019Review
- Review
- Article
- Nuclear IGF-1R predicts chemotherapy and targeted therapy resistance in metastatic colorectal cancer.British journal of cancer · 2017Article
- SUMOylation regulates nuclear accumulation and signaling activity of the soluble intracellular domain of the ErbB4 receptor tyrosine kinase.The Journal of biological chemistry · 2017Article
- Pias3 is necessary for dorso-ventral patterning and visual response of retinal cones but is not required for rod photoreceptor differentiation.Biology open · 2017Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ErbB4 is a receptor tyrosine kinase implicated in the development and homeostasis of the heart, central nervous system, and mammary gland. Cleavable isoforms of ErbB4 release a soluble intracellular domain (ICD) that can translocate to the nucleus and function as a transcriptional coregulator. In search of regulatory mechanisms of ErbB4 ICD function, we identified PIAS3 as a novel interaction partner of ErbB4 ICD. In keeping with the small ubiquitin-like modifier (SUMO) E3 ligase function of protein inhibitor of activated STAT (PIAS) proteins, we showed that the ErbB4 ICD is modified by SUMO, and that PIAS3 stimulates the SUMOylation. Upon overexpression of PIAS3, the ErbB4 ICD generated from the full-length receptor accumulated into the nucleus in a manner that was dependent on the functional nuclear localization signal of ErbB4. In the nucleus, ErbB4 colocalized with PIAS3 and SUMO-1 in promyelocytic leukemia nuclear bodies, nuclear domains involved in regulation of transcription. Accordingly, PIAS3 overexpression had an effect on the transcriptional coregulatory activity of ErbB4, repressing its ability to coactivate transcription with Yes-associated protein. Finally, knockdown of PIAS3 with siRNA partially rescued the inhibitory effect of the ErbB4 ICD on differentiation of MDA-MB-468 breast cancer and HC11 mammary epithelial cells. Our findings illustrate that PIAS3 is a novel regulator of ErbB4 receptor tyrosine kinase, controlling its nuclear sequestration and function.
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