High impact information on DEPDC2

• The contact interface between the PH domain of P-Rex2 and Rac1 involves the switch loop and helix 3 of Rac1 [1].
• Despite having the ability to recognize this chimeric Cdc42, P-Rex2 is unable to catalyze nucleotide exchange on Cdc42, suggesting that recognition of substrate and catalysis are two distinct events [1].
• P-Rex1 is mainly expressed in neutrophils and regulates reactive oxygen species formation in these cells (Welch et al., 2002), whereas P-Rex2 is expressed in a wide variety of tissues but not in neutrophils (Donald et al., 2004), and P-Rex2B is expressed in the heart (Rosenfeldt et al., 2004) [2].

Associations of DEPDC2 with chemical compounds

• P-Rex1 and P-Rex2 also contain two DEP and two PDZ protein interaction domains, as well as homology over their COOH-terminal half to inositol polyphosphate 4-phosphatase (Donald et al., 2004; Welch et al., 2002) [2].

References