TC-PTP dephosphorylates the guanine nucleotide exchange factor C3G (RapGEF1) and negatively regulates differentiation of human neuroblastoma cells

• Main Authors: Mitra A., Kalayarasan S., Gupta V., Radha V.
• Other Authors: MECHANOBIOLOGY INSTITUTE
• Format: Article
• Published: 2019
• Subjects: forskolin; guanine nucleotide exchange factor; guanine nucleotide exchange factor C3G; non receptor protein tyrosine phosphatase 2; pervanadate; phosphotyrosine; somatomedin; tyrosine; unclassified drug; vanadic acid; mutant protein; protein tyrosine kinase; PTPN2 protein, human; animal cell; article; binding assay; carboxy terminal sequence; complex formation; controlled study; embryo; enzyme inactivation; enzyme substrate; Golgi complex; human; human cell; in vitro study; in vivo study; nerve cell differentiation; nerve fiber growth; neuroblastoma; neuroblastoma cell; nonhuman; nucleotide binding site; oncogene src; protein dephosphorylation; protein expression; protein function; protein localization; protein phosphorylation; protein protein interaction; cell differentiation; cell strain HEK293; chemistry; drug effect; enzymology; metabolism; neurite; pathology; phosphorylation; protein binding; protein tertiary structure; protein transport; structure activity relation; tumor cell line; Cell Differentiation; Cell Line, Tumor; Forskolin; Golgi Apparatus; Guanine Nucleotide-Releasing Factor 2; HEK293 Cells; Humans; Mutant Proteins; Neurites; Neuroblastoma; Phosphorylation; Phosphotyrosine; Protein Binding; Protein Structure, Tertiary; Protein Transport; Protein Tyrosine Phosphatase, Non-Receptor Type 2; src-Family Kinases; Structure-Activity Relationship; Vanadates
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/162035
• Institution: National University of Singapore

10.1371/journal.pone.0023681