Endogenous arginine-specific ADP-ribosyltransferases and target proteins.
We investigated vertebrate arginine-specific ADP-ribosyltransferases and target proteins for the enzyme. ADP-ribosyltransferase found in each organelle ADP-ribosylated preferentially an endogenous acceptor protein co-localized with the enzyme. We propose that the ADP-ribosylation of tissue-specific target protein by the endogenous ADP-ribosyltransferase may participate in the regulation of cellular processes, including signal transduction.
Shimoyama
M
M
Department of Biochemistry, Shimane Medical University, Izumo, Japan.
Tsuchiya
M
M
D036002:ADP Ribose Transferases / Q000378:metabolism*; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism; D000262:Adenylyl Cyclases / Q000378:metabolism; D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D000252:Calcium-Transporting ATPases / Q000378:metabolism*; D002645:Chickens; D019204:GTP-Binding Proteins / Q000378:metabolism*; D009132:Muscles / Q000201:enzymology; D011817:Rabbits; D013154:Spleen / Q000201:enzymology / Q000378:metabolism
D001798:Blood Proteins; D000246:Adenosine Diphosphate Ribose; D036002:ADP Ribose Transferases; D019204:GTP-Binding Proteins; D000262:Adenylyl Cyclases; D000252:Calcium-Transporting ATPases