ArticleCell communication and signaling : CCS2006
Serine phosphorylation regulates paxillin turnover during cell migration.
Article in Cell communication and signaling : CCS, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Fyn-Mediated Paxillin Tyrosine 31 Phosphorylation Regulates Migration and Invasion of Breast Cancer Cells.International journal of molecular sciences · 2023Article
- The Role of Paxillin Aberrant Expression in Cancer and Its Potential as a Target for Cancer Therapy.International journal of molecular sciences · 2023Review
- Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021Review
- In Utero Exposure to a High-Fat Diet Programs Hepatic Hypermethylation and Gene Dysregulation and Development of Metabolic Syndrome in Male Mice.Endocrinology · 2017Article
- Endosomal sorting and c-Cbl targeting of paxillin to autophagosomes regulate cell-matrix adhesion turnover in human breast cancer cells.Oncotarget · 2017Article
- Paxillin: a crossroad in pathological cell migration.Journal of hematology & oncology · 2017Review
- Review
- Autophagy Promotes Focal Adhesion Disassembly and Cell Motility of Metastatic Tumor Cells through the Direct Interaction of Paxillin with LC3.Cell reports · 2016Article
- The β isoform of GSK3 mediates podocyte autonomous injury in proteinuric glomerulopathy.The Journal of pathology · 2016Article
- Smooth Muscle Stiffness Sensitivity is Driven by Soluble and Insoluble ECM Chemistry.Cellular and molecular bioengineering · 2015Article
- SATB2 enhances migration and invasion in osteosarcoma by regulating genes involved in cytoskeletal organization.Oncogene · 2015Article
- MicroRNA-145 suppresses cell migration and invasion by targeting paxillin in human colorectal cancer cells.International journal of clinical and experimental pathology · 2015Article
- Glycogen synthase kinase 3β dictates podocyte motility and focal adhesion turnover by modulating paxillin activity: implications for the protective effect of low-dose lithium in podocytopathy.The American journal of pathology · 2014Article
- SLK-mediated phosphorylation of paxillin is required for focal adhesion turnover and cell migration.Oncogene · 2013Article
- Identification of IGPR-1 as a novel adhesion molecule involved in angiogenesis.Molecular biology of the cell · 2012Article
- Paxillin and hydrogen peroxide-inducible clone 5 expression and distribution in control and Alzheimer disease hippocampi.Journal of neuropathology and experimental neurology · 2010Article
- Paxillin comes of age.Journal of cell science · 2008Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPaxillin acts as an adaptor protein that localizes to focal adhesion. This protein is regulated during cell migration by phosphorylation on tyrosine, serine and threonine residues. Most of these phosphorylations have been implicated in the regulation of different steps of cell migration. The two major phosphorylation sites of paxillin in response to adhesion to an extracellular matrix are serines 188 and 190. However, the function of this phosphorylation event remains unknown. The purpose of this work was to determine the role of paxillin phosphorylation on residues S188 and S190 in the regulation of cell migration.
resultsWe used NBT-II epithelial cells that can be induced to migrate when plated on collagen. To examine the role of paxillin serines 188/190 in cell migration, we constructed an EGFP-tagged paxillin mutant in which S188/S190 were mutated into unphosphorylatable alanine residues. We provide evidence that paxillin is regulated by proteasomal degradation following polyubiquitylation of the protein. During active cell migration on collagen, paxillin is protected from proteasome-dependent degradation. We demonstrate that phosphorylation of serines 188/190 is necessary for the protective effect of collagen. In an effort to understand the physiological relevance of paxillin protection from degradation, we show that cells expressing the paxillin S188/190A interfering mutant spread less, have reduced protrusive activity but migrate more actively.
conclusionOur data demonstrate for the first time that serine-regulated degradation of paxillin plays a key role in the modulation of membrane dynamics and consequently, in the control of cell motility.
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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.