Mouse anti-Human sapiens (Human) ECT2 Monoclonal Antibody

Function

Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death

Subcellular Location

Nucleus; Cytoplasm; Cytoplasm, cytoskeleton, spindle; Cleavage furrow; Midbody; Cell junction; Cell junction, tight junction; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome

Tissue Specificity

Expressed in lung epithelial cells (at protein level). Expressed in squamous cell carcinoma, primary non-small cell lung cancer tumors and lung adenocarcinoma

Subunit

Homodimer (PubMed:14645260, PubMed:15545273, PubMed:16170345). Homooligomer (PubMed:15545273). Found in the centralspindlin complex (PubMed:16236794). Interacts with NR1I3 (By similarity). Interacts (Thr-359 phosphorylated form) with PARD6A; the interaction is observed in cancer cells (PubMed:15254234, PubMed:19617897). Interacts (Thr-359 phosphorylated form) with PRKCI; the interaction is observed in cancer cells (PubMed:19617897). Interacts with PKP4; the interaction is observed at the midbody (PubMed:22814378). Interacts with RACGAP1/CYK4; the interaction is direct, occurs in a microtubule-dependent manner, occurs at anaphase and during cytokinesis, is inhibited in metaphase by phosphorylation of ECT2 on Thr-373 and is stimulated in early anaphase by dephosphorylation of ECT2 probably on Thr-373 through CDK1 activity (PubMed:16103226, PubMed:16129829, PubMed:16236794, PubMed:19468300, PubMed:19468302, PubMed:25068414). Interacts with PLK1; the interaction is stimulated upon its phosphorylation on Thr-444 (PubMed:16247472). Interacts with RHOA; the interaction results in allosteric activation of ECT2 (PubMed:31888991). Interacts with KIF23, PARD3, PARD6B and PRKCQ (PubMed:15254234, PubMed:16236794). Interacts with NEDD9/HEF1 (PubMed:16394104)

• Tatsumoto T. et al. Human ECT2 is an exchange factor for Rho GTPases, phosphorylated in G2/M phases, and involved in cytokinesis. — J. Cell Biol. (1999)
• Saito S. et al. Rho exchange factor ECT2 is induced by growth factors and regulates cytokinesis through the N-terminal cell cycle regulator-related domains. — J. Cell. Biochem. (2003)
• Wolf A. et al. The armadillo protein p0071 regulates Rho signalling during cytokinesis. — Nat. Cell Biol. (2006)
• Ota T. et al. Complete sequencing and characterization of 21,243 full-length human cDNAs. — Nat. Genet. (2004)
• Muzny D.M. et al. The DNA sequence, annotation and analysis of human chromosome 3. — Nature (2006)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Bechtel S. et al. The full-ORF clone resource of the German cDNA consortium. — BMC Genomics (2007)
• Saito S. et al. Deregulation and mislocalization of the cytokinesis regulator ECT2 activate the Rho signaling pathways leading to malignant transformation. — J. Biol. Chem. (2004)