ArticleMolecular endocrinology (Baltimore, Md.)2013
Tyrosyl phosphorylated PAK1 regulates breast cancer cell motility in response to prolactin through filamin A.
Article in Molecular endocrinology (Baltimore, Md.), 2013. 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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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.
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Who cites it
28 citing papers in PubMed, 38 citations in OpenAlex.
- Centrosomal JAK2 Tyrosine Kinase Regulates Primary Cilia Length, Cell Proliferation, and Cilia Orientation During Cell Migration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Filamin a binds deleted in liver cancer 1 (DLC1) to promote its tumor suppressor activity and inhibit the SRF coactivator MRTF-A.Neoplasia (New York, N.Y.) · 2026Article
- Modulating PAK1: Accessory Proteins as Promising Therapeutic Targets.Biomolecules · 2025Review
- Role of Filamin A in Growth and Migration of Breast Cancer-Review.Current issues in molecular biology · 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
- The SH2 domain and kinase activity of JAK2 target JAK2 to centrosome and regulate cell growth and centrosome amplification.PloS one · 2022Article
- NudC L279P Mutation Destabilizes Filamin A by Inhibiting the Hsp90 Chaperoning Pathway and Suppresses Cell Migration.Frontiers in cell and developmental biology · 2021Article
- Periostin/Filamin-A: A Candidate Central Regulatory Axis for Valve Fibrogenesis and Matrix Compaction.Frontiers in cell and developmental biology · 2021Article
- Mechanical Cues Affect Migration and Invasion of Cells From Three Different Directions.Frontiers in cell and developmental biology · 2020Review
- Molecular Tuning of Filamin A Activities in the Context of Adhesion and Migration.Frontiers in cell and developmental biology · 2020Review
- Alpha-actinin 4 and tumorigenesis of hepatocellular carcinoma.Translational cancer research · 2019Article
- The Role of PAK1 in the Maturation of Invadopodia During Transient Mechanical Stimulation.Frontiers in cell and developmental biology · 2019Article
- Engineering Pak1 Allosteric Switches.ACS synthetic biology · 2017Article
- Prolactin-induced PAK1 tyrosyl phosphorylation promotes FAK dephosphorylation, breast cancer cell motility, invasion and metastasis.BMC cell biology · 2016Article
- Prolactin Signaling Stimulates Invasion via Na(+)/H(+) Exchanger NHE1 in T47D Human Breast Cancer Cells.Molecular endocrinology (Baltimore, Md.) · 2016Article
- 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
- Filamin A: Insights into its Exact Role in Cancers.Pathology oncology research : POR · 2016Review
- Potentially functional polymorphisms in PAK1 are associated with risk of lung cancer in a Chinese population.Cancer medicine · 2015Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The p21-activated serine-threonine kinase (PAK1) is activated by small GTPase-dependent and -independent mechanisms and regulates cell motility. Both PAK1 and the hormone prolactin (PRL) have been implicated in breast cancer by numerous studies. We have previously shown that the PRL-activated tyrosine kinase JAK2 (Janus tyrosine kinase 2) phosphorylates PAK1 in vivo and identified tyrosines (Tyr) 153, 201, and 285 in the PAK1 molecule as sites of JAK2 tyrosyl phosphorylation. Here, we have used human breast cancer T47D cells stably overexpressing PAK1 wild type or PAK1 Y3F mutant in which Tyr(s) 153, 201, and 285 were mutated to phenylalanines to demonstrate that phosphorylation of these three tyrosines are required for maximal PRL-dependent ruffling. In addition, phosphorylation of these three tyrosines is required for increased migration of T47D cells in response to PRL as assessed by two independent motility assays. Finally, we show that PAK1 phosphorylates serine (Ser) 2152 of the actin-binding protein filamin A to a greater extent when PAK1 is tyrosyl phosphorylated by JAK2. Down-regulation of PAK1 or filamin A abolishes the effect of PRL on cell migration. Thus, our data presented here bring some insight into the mechanism of PRL-stimulated motility of breast cancer cells.
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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 Socratic graph.