[Analysis of GEF activity of Bcr protein DH domain].
Dbl protein and DH (Dbl homology) domains are key regulators of RhoGTPases and promote GDP release from the complex with GTPase. About 70 DH-containing proteins are found. DH domain is localized in tandem with PH (pleckstrin homology) domain in many proteins. Bcr protein is a partner of Abl in reciprocal translocation t(9;22) which leads to Philadelphia chromosome formation. In the present study we have cloned Bcr DH and PH domains into the vector for mammalian expression. GEF activity of Bcr DH domain was studied alone and together with PH domain. Our data suggest, that Bcr DH domains does not reveal GEF activity against RhoGTPases RhoA, Cdc42 and Racl subfamilies in vivo.
Miroshnychenko
D O
DO
Teleheiev
H D
HD
Maliuta
S S
SS
D000595:Amino Acid Sequence; D002460:Cell Line; D016044:Fusion Proteins, bcr-abl / Q000235:genetics*; D020662:Guanine Nucleotide Exchange Factors / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D010677:Philadelphia Chromosome; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014162:Transfection; D020741:rho GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*
D020662:Guanine Nucleotide Exchange Factors; D016044:Fusion Proteins, bcr-abl; D020741:rho GTP-Binding Proteins