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Literature summary for 1.14.11.2 extracted from

  • Vogel, S.; Wottawa, M.; Farhat, K.; Zieseniss, A.; Schnelle, M.; Le-Huu, S.; von Ahlen, M.; Malz, C.; Camenisch, G.; Katschinski, D.M.
    Prolyl hydroxylase domain (PHD) 2 affects cell migration and F-actin formation via RhoA/rho-associated kinase-dependent cofilin phosphorylation (2010), J. Biol. Chem., 285, 33756-33763.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
H131A/D315A inactive mutant Homo sapiens
additional information transient transfection of HeLa and A549 cells with siRNA-targeting PHD2 or PHD3, transient downregulation of PHD3 in HeLa cells or transfection of the control siRNA does not affect the phosphorylation of Cof-1, downregulation of PHD2 leads to an increase of phosphorylated Cof-1. Induction of a PHD2 knockdown in tetracycline-inducible HeLa PHD2 knockdown cells, 1B6 and 3B7 cells from cell line 2.1.1-16, results in increased F-actin formation as detected by phalloidin staining. PHD2 knockdown impairs cell migration. Wild-type PHD2 reverses the increased p-Cof1 levels in 3B7 cells, whereas the mutant PHD2 has no similar effect Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Synonyms

Synonyms Comment Organism
prolyl hydroxylase
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Homo sapiens
prolyl-4-hydroxylase
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Homo sapiens

Expression

Organism Comment Expression
Homo sapiens PHD2 is hypoxia-inducible by HIF-1alpha up

General Information

General Information Comment Organism
physiological function PHD2 mediates F-actin assembly involving inhibition of Cof-1 phosphorylation. Isozyme PHD2 is the main isoform regulating HIF-1alpha hydroxylation and thus stability in normoxia Homo sapiens