TRBs are newly emerged three member family proteins including: TRB1 TRB2 and TRB3. TRB family members are characterized by a strong homology to the kinase domain of Ser/Thr protein kinases. Since they lack an ATP binding domain and contain a variant catalytic core motif, TRBs do not function as a protein kinase. TRBs bind to Akt and inhibit Akt activation. TRB expression is enhanced during apoptosis as well as cell differentiation. TRB3 forms heterodimers with both TRB1 and TRB2. Remarkably, none of the TRBs form a homodimer nor do TRB1 and TRB2 form a heterodimer. Our future research is to elucidate the functional and structural importance of the TRB family members in cell differentiation, apoptosis.

TRBs bind to Akt and inhibit Akt activation. TRB expression is enhanced during apoptosis as well as cell differentiation. TRB3 forms heterodimers with both TRB1 and TRB2. Remarkably, none of the TRBs form a homodimer nor do TRB1 and TRB2 form a heterodimer. Our research will a) explore the role of TRB3 in muscle cell differentiation. We will also analyze how TRB3 modulates muscle cell specific gene expression. b) address the mechanism by which the expression of TRB3 is regulated. We will identify promoter sequences and other genetic elements required for the regulation of TRB expression cell differentiation. c) determine the structural and functional requirements for the heterodimerization of TRB3 with TRB1 and TRB2 and explore the structural and functional requirements for the interaction between Akt family members and TRB family members, as well as the functional outcome of these interactions.

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Glucose is a fundamental source of energy for all eukaryotic cells. In humans, all cells use glucose for their energy needs. Abnormal glucose metabolism usually associates with insulin-resistance, the hallmark of Type II Diabetes. To understand the functional importance of Akt, we have isolated a novel Akt interaction protein, Aclip.