Mitochondrial calcium binding protein

Hubbard, M.J., McHugh, N.J. (1996). Mitochondrial ATP synthase F-l-beta-subunit is a calcium-binding protein. FEBSLett. 391 323-9. 

Mikkelson, R.B. Wallach, D.F.H. (1976) Binding of Fluorescent Lanthanides to Rat Liver Mitochondrial Membranes and Calcium Ion-binding Proteins , Biochimica et Biophysica Acta, 433, 674-83... 

Although the importance of the nuclear T3 receptor is well established, there also is evidence for the existence of non-nuclear T3 receptors. For example, Segal and Ingbar46 demonstrated an immediate T3-mediated increase in calcium accumulation in rat thymocytes, an increase that was insensitive to inhibitors of protein biosynthesis. A direct effect on oxidative phosphorylation has been suggested to result from T3 binding to saturable receptors of mitochondrial membranes. The possible roles of non-nuclear T3 receptors have been reviewed by Sterling47. 

The TRADD or FADD domains bind to adapter proteins in the cytosol and together they form of a death inducing signaling complex (DISC). This complex recruits caspase-8, one of a family of calcium ion-activated serine proteases (caspases) which cleave polypeptides on the C-terminal side of their aspartate residues. DISC activates caspase-8 to activate a Bcl-2 activator, BID (Fig. 13.1 Oa). The resultant tBid fragment activates effector Bcl-2 proteins on the endoplasmic reticular membrane and mitochondrial outer membrane. 

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