ArticleCellular signalling2009
Characterization of EVL-I as a protein kinase D substrate.
Article in Cellular signalling, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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The trial behind it
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Who cites it
15 citing papers in PubMed, 20 citations in OpenAlex.
- Review
- EVL regulates VEGF receptor-2 internalization and signaling in developmental angiogenesis.EMBO reports · 2021Article
- NKG2D-DAP10 signaling recruits EVL to the cytotoxic synapse to generate F-actin and promote NK cell cytotoxicity.Journal of cell science · 2019Article
- Protein kinase D2: a versatile player in cancer biology.Oncogene · 2018Review
- Peptide array-based screening reveals a large number of proteins interacting with the ankyrin-repeat domain of the zDHHC17The Journal of biological chemistry · 2017Article
- The phosphorylation status of VASP at serine 322 can be predictive for aggressiveness of invasive ductal carcinoma.Oncotarget · 2015Article
- Protein kinase d isoforms differentially modulate cofilin-driven directed cell migration.PloS one · 2014Article
- Protein kinase D1-mediated phosphorylations regulate vasodilator-stimulated phosphoprotein (VASP) localization and cell migration.The Journal of biological chemistry · 2013Article
- Protein kinase D isoforms: new targets for therapy in invasive breast cancers?Expert review of anticancer therapy · 2013Article
- Protein kinase D regulates RhoA activity via rhotekin phosphorylation.The Journal of biological chemistry · 2012Article
- Protein kinase D regulates cofilin activity through p21-activated kinase 4.The Journal of biological chemistry · 2011Article
- Article
- Protein kinase D as a potential new target for cancer therapy.Biochimica et biophysica acta · 2010Review
- Article
- Regulation of VASP by phosphorylation: consequences for cell migration.Cell adhesion & migrationArticle
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
EVL-I is a splice variant of EVL (Ena/VASP like protein), whose in vivo function and regulation are still poorly understood. We found that Protein Kinase D (PKD) interacts in vitro and in vivo with EVL-I and phosphorylates EVL-I in a 21 amino acid alternately-included insert in the EVH2 domain. Following knockdown of the capping protein CPbeta and spreading on laminin, phosphorylated EVL-I can support filopodia formation and the phosphorylated EVL-I is localized at filopodial tips. Furthermore, we found that the lamellipodial localization of EVL-I is unaffected by phosphorylation, but that impairment of EVL-I phosphorylation is associated with ruffling of lamellipodia upon PDBu stimulation. Besides the lamellipodial and filopodial localization of phosphorylated EVL-I in fibroblasts, we determined that EVL-I is hyperphosphorylated and localized in the cell-cell contacts of certain breast cancer cells and mouse embryo keratinocytes. Taken together, our results show that phosphorylated EVL-I is present in lamellipodia, filopodia and cell-cell contacts and suggest the existence of signaling pathways that may affect EVL-I via phosphorylation of its EVH2 domain.
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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.