Cayman ECT2 BRCT domains (human, recombinant)

Epithelial cell-transforming sequence 2 oncogene (ECT2) is a guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP from small GTPases of the Rho family, such as RhoA, RhoC, Rac1, and Cdc42. ECT2 GEF activity plays an essential role during cytokinesis. ECT2 contains a DH (DBL-homology) domain, a pleckstrin homology (pH) domain and tandem BRCT domains. BRCT domains are modular units of ~100 amino acids that fold independently and recognize linear phosphoserine or phosphothreonine regions to mediate protein-protein and protein-DNA interactions.^, BRCT domains were initially recognized in the C-terminal region of the breast cancer protein BRCA1, as well as the p53 binding protein and the yeast cell cycle checkpoint protein RAD9. BRCT domains often occur as tandem repeats at the C-terminal end of several proteins that are functionally diverse. Most BRCT domain-containing proteins participate in DNA-damage checkpoint control or DNA-repair pathways, or both.^, The BRCT domains of ECT2 make intramolecular interactions with the C-terminal DH/pH domains of the protein, thus, masking the catalytic GEF activity for Rho GTPases. Additionally, release of the autoinhibition by the BRCT domains may be necessary for the proper functioning of ECT2 during cytokinesis. Expression levels of ECT have been shown to be strongly correlated with prognosis in glioma patients.

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