The bioenergetics of Golgi apparatus function: evidence for an ATP-dependent proton pump.
The energy requirement for the processing of newly-synthesized proteins by the Golgi was examined. Rat liver Golgi preparations enriched more than 100-fold have high ATPase activity that co-purified with the Golgi marker enzyme galactosyl transferase. The ATPase activity was 80% inhibited by dicyclohexylcarbodiimide and may represent a proton pump. Evidence is presented for a functional role of the ATPase in Golgi. First, measurement of [14C]methylamine uptake demonstrated ATP-dependent acidification. Second, inhibition of the ATPase with dicyclohexylcarbodiimide resulted in a 3-fold accumulation of newly-synthesized protein in the Golgi.
D000251:Adenosine Triphosphatases / Q000302:isolation & purification / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D005700:Galactosyltransferases / Q000302:isolation & purification / Q000378:metabolism; D006056:Golgi Apparatus / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000201:enzymology*; D051381:Rats
D000255:Adenosine Triphosphate; D005700:Galactosyltransferases; D000251:Adenosine Triphosphatases