ArticlePloS one2011
Role of palladin phosphorylation by extracellular signal-regulated kinase in cell migration.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Signs of Problematic Internet use Affect Resting-State EEG Microstates.Brain topography · 2025Article
- EphA2 regulates vascular permeability and prostate cancer metastasis via modulation of cell junction protein phosphorylation.Oncogene · 2025Article
- Palladin isoforms 3 and 4 regulate cancer-associated fibroblast pro-tumor functions in pancreatic ductal adenocarcinoma.Scientific reports · 2021Article
- The Role of Palladin in Podocytes.Journal of the American Society of Nephrology : JASN · 2018Article
- Actin Dysfunction Induces Cell Cycle Delay at G2/M with Sustained ERK and RSK Activation in IMR-90 Normal Human Fibroblasts.Molecules and cells · 2018Article
- PP2A binds to the LIM domains of lipoma-preferred partner through its PR130/B″ subunit to regulate cell adhesion and migration.Journal of cell science · 2016Article
- Dual roles of palladin protein in in vitro myogenesis: inhibition of early induction but promotion of myotube maturation.PloS one · 2015Article
- Actin-associated protein palladin promotes tumor cell invasion by linking extracellular matrix degradation to cell cytoskeleton.Molecular biology of the cell · 2014Article
- Actin binding proteins, spermatid transport and spermiation.Seminars in cell & developmental biology · 2014Review
- Serines in the intracellular tail of podoplanin (PDPN) regulate cell motility.The Journal of biological chemistry · 2013Article
- Mitogen-Activated Protein (MAP) Kinase Scaffolding Proteins: A Recount.International journal of molecular sciences · 2013Article
- Actin cross-linking protein palladin and spermatogenesis.Spermatogenesis · 2013Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphorylation of actin-binding proteins plays a pivotal role in the remodeling of the actin cytoskeleton to regulate cell migration. Palladin is an actin-binding protein that is phosphorylated by growth factor stimulation; however, the identity of the involved protein kinases remains elusive. In this study, we report that palladin is a novel substrate of extracellular signal-regulated kinase (ERK). Suppression of ERK activation by a chemical inhibitor reduced palladin phosphorylation, and expression of active MEK alone was sufficient for phosphorylation. In addition, an in vitro kinase assay demonstrated direct palladin phosphorylation by ERK. We found that Ser77 and Ser197 are essential residues for phosphorylation. Although the phosphorylation of these residues was not required for actin cytoskeletal organization, we found that expression of non-phosphorylated palladin enhanced cell migration. Finally, we show that phosphorylation inhibits the palladin association with Abl tyrosine kinase. Taken together, our results indicate that palladin phosphorylation by ERK has an anti-migratory function, possibly by modulating interactions with molecules that regulate cell migration.
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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.