Rho-modifying C3-like ADP-ribosyltransferases.
C3-like exoenzymes comprise a family of seven bacterial ADP-ribosyltransferases, which selectively modify RhoA, B, and C at asparagine-41. Crystal structures of C3 exoenzymes are available, allowing novel insights into the structure-function relationships of these exoenzymes. Because ADP-ribosylation specifically inhibits the biological functions of the low-molecular mass GTPases, C3 exoenzymes are established pharmacological tools to study the cellular functions of Rho GTPases. Recent studies, however, indicate that the functional consequences of C3-induced ADP-ribosylation are more complex than previously suggested. In the present review the basic properties of C3 exoenzymes are briefly summarized and new findings are reviewed.
Aktories
K
K
Institute of Experimental and Clinical Pharmacology and Toxicology, Albert-Ludwigs University Freiburg, Otto-Krayer-Haus, Albertstr. 25, Freiburg, Germany. Klaus.Aktories@pharmakol.uni-freiburg.de.
Wilde
C
C
Vogelsgesang
M
M
D036002:ADP Ribose Transferases / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D001905:Botulinum Toxins / Q000378:metabolism*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D036002:ADP Ribose Transferases; C063007:exoenzyme C3, Clostridium botulinum; D001905:Botulinum Toxins