ArticleMolecular endocrinology (Baltimore, Md.)2011
PAK1-Nck regulates cyclin D1 promoter activity in response to prolactin.
Article in Molecular endocrinology (Baltimore, Md.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
24 citing papers in PubMed, 40 citations in OpenAlex.
- Modulating PAK1: Accessory Proteins as Promising Therapeutic Targets.Biomolecules · 2025Review
- Role of Cyclins and Cytoskeletal Proteins in Endometriosis: Insights into Pathophysiology.Cancers · 2024Review
- Prolactin-activated PAK1 potentiates estrogen response to breast cancer cell epithelial-mesenchymal transition, migration and invasion.microPublication biology · 2024Article
- Prolactin-induced tyrosyl phosphorylation of PAK1 facilitates epithelial-mesenchymal transition.microPublication biology · 2024Article
- Article
- circSFMBT1 promotes pancreatic cancer growth and metastasis via targeting miR-330-5p/PAK1 axis.Cancer gene therapy · 2021Article
- The metastatic promoter DEPDC1B induces epithelial-mesenchymal transition and promotes prostate cancer cell proliferation via Rac1-PAK1 signaling.Clinical and translational medicine · 2020Article
- PAK1, PAK1Δ15, and PAK2: similarities, differences and mutual interactions.Scientific reports · 2019Article
- Review
- Synergistic Activation of ERα by Estrogen and Prolactin in Breast Cancer Cells Requires Tyrosyl Phosphorylation of PAK1.Cancer research · 2016Article
- PAK1 translocates into nucleus in response to prolactin but not to estrogen.Biochemical and biophysical research communications · 2016Article
- LIM Kinase, a Newly Identified Regulator of Presynaptic Remodeling by Rod Photoreceptors After Injury.Investigative ophthalmology & visual science · 2015Article
- Article
- Tyrosyl phosphorylated serine-threonine kinase PAK1 is a novel regulator of prolactin-dependent breast cancer cell motility and invasion.Advances in experimental medicine and biology · 2015Review
- p21-Activated Kinases 1, 2 and 4 in Endometrial Cancers: Effects on Clinical Outcomes and Cell Proliferation.PloS one · 2015Article
- Republished: tracing PAKs from GI inflammation to cancer.Postgraduate medical journal · 2014Article
- The Role of Ect2 Nuclear RhoGEF Activity in Ovarian Cancer Cell Transformation.Genes & cancer · 2013Article
- PAK1 regulates breast cancer cell invasion through secretion of matrix metalloproteinases in response to prolactin and three-dimensional collagen IV.Molecular endocrinology (Baltimore, Md.) · 2013Article
- p-21-Activated kinase 1 mediates gastrin-stimulated proliferation in the colorectal mucosa via multiple signaling pathways.American journal of physiology. Gastrointestinal and liver physiology · 2013Article
- Tyrosyl phosphorylated PAK1 regulates breast cancer cell motility in response to prolactin through filamin A.Molecular endocrinology (Baltimore, Md.) · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Prolactin (PRL) is critical for alveolar proliferation and differentiation in normal mammary development and is also implicated in breast cancer. PRL influences cell proliferation and growth by altering the expression of cyclin D1. Cyclin D1 expression is directly regulated by PRL through the Janus kinase 2 (JAK2)/signal transducer and activator of transcription 5-mediated transcriptional activation of the cyclin D1 promoter. A p21-activated serine-threonine kinase (PAK)1 has also been implicated in the regulation of cyclin D1 gene expression. We have previously demonstrated that JAK2 directly phosphorylates PAK1 and extend these data here to demonstrate that PAK1 activates the cyclin D1 promoter in response to PRL. We show that mutation of PAK1 Tyr 153, 201, and 285 (sites of JAK2 phosphorylation; PAK1 Y3F) decreases both PAK1 nuclear translocation in response to PRL and PRL-induced cyclin D1 promoter activity by 55%. Mutation of the PAK1 nuclear localization signals decreases PRL-induced cyclin D1 promoter activity by 46%. A PAK1 Y3F mutant lacking functional nuclear localization signals decreases PRL-induced cyclin D1 activity by 68%, suggesting that there is another PAK1-dependent mechanism to activate the cyclin D1 promoter. We have found that adapter protein Nck sequesters PAK1 in the cytoplasm and that coexpression of both PAK1 and Nck inhibits the amplifying effect of PRL-induced PAK1 on cyclin D1 promoter activity (95% inhibition). This inhibition is partially abolished by disruption of PAK1-Nck binding. We propose two PAK1-dependent mechanisms to activate cyclin D1 promoter activity in response to PRL: via nuclear translocation of tyrosyl-phosphorylated PAK1 and via formation of a Nck-PAK1 complex that sequesters PAK1 in the cytoplasm.
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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.