Author/Editor		Deželak, Matjaž; Bavec, Aljoša
Title		Glucagon like-peptide-1 receptor is covalently modified by endogenous mono-ADP-ribosyltransferase
Type		članek
Source		Mol Biol Rep
Vol. and No.		Letnik 39, št. 4
Publication year		2012
Volume		str. 4375-81
Language		eng
Abstract		Our previous study revealed a mono-ADP-ribosyltransferase mediated in vitro mono-ADP-ribosylation of IC(3) peptide, a peptide with sequence corresponded to third intracellular loop of glucagon like-peptide-1 (GLP-1) receptor. Furthermore, Arg(348) was shown to be modified amino acid residue although its mutation did not eliminate mono-ADP-ribosylation completely. In order to further study the signaling mechanisms of GLP-1 receptor, we took on lease a possibility that an alternative site of enzymatic modification exist so mono-ADP-ribosylation of Cys(341) was hypothesized. The results confirmed both Arg(348) and Cys(341) as a site of mono-ADP-ribosylation where Arg(348) is modified predominantly. Sum of mono-ADP-ribosylation rate of both single IC(3) mutants coincided with IC(3) rate. What is in vivo role of Cys(341) mono-ADP-ribosylation is entirely speculative but our study represents an important step toward a complete understanding of signaling via GLP-1 receptor.
Descriptors		GLUCAGON RECEPTORS, GLUCAGON CHO CELLS NAD+ ADP-RIBOSYLTRANSFERASE NAD(P)(+)-ARGININE ADP-RIBOSYLTRANSFERASE TRANSLATION, GENETIC IMMUNOBLOTTING DIABETES MELLITUS