ArticleThe Journal of biological chemistry2015
Subcellular localization and Ser-137 phosphorylation regulate tumor-suppressive activity of profilin-1.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Lentivirus enables the detection of strand-specific ssDNA gaps by the DNA fiber spreading assay.Communications biology · 2026Article
- RAGE Axis in the Pathogenesis and Treatment of CNS Neurodegeneration in Long-Term Hyperglycemia.International journal of molecular sciences · 2026Review
- Loss of Nuclear Profilin 1 Triggers Oncogenic Reprogramming of Mammary Epithelial Cells Through Dysregulated DNA Replication in Breast Cancer.Journal of breast cancer · 2025Article
- Cytoskeleton dysfunction of motor neuron in spinal muscular atrophy.Journal of neurology · 2024Review
- Profilin-1 regulates DNA replication forks in a context-dependent fashion by interacting with SNF2H and BOD1L.Nature communications · 2022Article
- Phospho-SerCancers · 2021Article
- Measuring expression heterogeneity of single-cell cytoskeletal protein complexes.Nature communications · 2021Article
- Serum levels of cytoskeleton remodeling proteins and their mRNA expression in tumor tissue of metastatic laryngeal and hypopharyngeal cancers.Molecular biology reports · 2021Article
- The role of profilin-1 in cardiovascular diseases.Journal of cell science · 2021Review
- Cancer-associated exportin-6 upregulation inhibits the transcriptionally repressive and anticancer effects of nuclear profilin-1.Cell reports · 2021Article
- Profilin-1; a novel regulator of DNA damage response and repair machinery in keratinocytes.Molecular biology reports · 2021Article
- SerFrontiers in cell and developmental biology · 2021Article
- Profilin: many facets of a small protein.Biophysical reviews · 2020Review
- Phospho-SerCell reports · 2020Article
- Cofilin and profilin: partners in cancer aggressiveness.Biophysical reviews · 2018Review
- A loss of profilin-1 in late-stage oral squamous cell carcinoma.Journal of oral pathology & medicine : official publication of the International Association of Oral Pathologists and the American Academy of Oral Pathology · 2017Article
- Protein kinase A-mediated phosphorylation of the Broad-Complex transcription factor in silkworm suppresses its transcriptional activity.The Journal of biological chemistry · 2017Article
- PFN2, a novel marker of unfavorable prognosis, is a potential therapeutic target involved in esophageal squamous cell carcinoma.Journal of translational medicine · 2016Article
- Profilin-1 mediated cell-cycle arrest: searching for drug targets.Cell cycle (Georgetown, Tex.) · 2015Article
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
Abstract
The actin-binding protein profilin-1 (Pfn1) inhibits tumor growth and yet is also required for cell proliferation and survival, an apparent paradox. We previously identified Ser-137 of Pfn1 as a phosphorylation site within the poly-l-proline (PLP) binding pocket. Here we confirm that Ser-137 phosphorylation disrupts Pfn1 binding to its PLP-containing ligands with little effect on actin binding. We find in mouse xenografts of breast cancer cells that mimicking Ser-137 phosphorylation abolishes cell cycle arrest and apoptotic sensitization by Pfn1 and confers a growth advantage to tumors. This indicates a previously unrecognized role of PLP binding in Pfn1 antitumor effects. Spatial restriction of Pfn1 to the nucleus or cytoplasm indicates that inhibition of tumor cell growth by Pfn1 requires its nuclear localization, and this activity is abolished by a phosphomimetic mutation on Ser-137. In contrast, cytoplasmic Pfn1 lacks inhibitory effects on tumor cell growth but rescues morphological and proliferative defects of PFN1 null mouse chondrocytes. These results help reconcile seemingly opposed cellular effects of Pfn1, provide new insights into the antitumor mechanism of Pfn1, and implicate Ser-137 phosphorylation as a potential therapeutic target for breast cancer.
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