ATPases trafficking, Menkes

Petris, M., Mercer, J., Culvenor, J., Lockhart, P, Glesson, P, and Camakaris, J. (1996). Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane A novel mechanism of regulated trafficking. EMBO J. 15, 101-112. 

The mechanisms of catalysis and copper-dependent trafficking of the Menkes protein have been summarized in a recent review. Biochemical studies indicated that mutation of six metal-binding sites did not abolish the catalytic activity of Menkes ATPase and hence it was considered that these motifs were not essential for copper translocation. However, the binding of copper to these sites increased the affinity of the protein for copper translocation, which would involve the interaction between the binding sites and the cytosohc ATP-binding domain of ATP7A. Much further work is necessary to delineate the mechanism of this process. 

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