Glucagon like-peptide-1 receptor is covalently modified by endogenous mono-ADP-ribosyltransferase |
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Authors: | Matja? De?elak Aljo?a Bavec |
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Institution: | (1) Institute of Biochemistry, Faculty of Medicine, University of Ljubljana, Vrazov trg 2, 1000 Ljubljana, Slovenia; |
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Abstract: | Our previous study revealed a mono-ADP-ribosyltransferase mediated in vitro mono-ADP-ribosylation of IC3 peptide, a peptide with sequence corresponded to third intracellular loop of glucagon like-peptide-1 (GLP-1) receptor. Furthermore,
Arg348 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 Cys341 was hypothesized. The results confirmed both Arg348 and Cys341 as a site of mono-ADP-ribosylation where Arg348 is modified predominantly. Sum of mono-ADP-ribosylation rate of both single IC3 mutants coincided with IC3 rate. What is in vivo role of Cys341 mono-ADP-ribosylation is entirely speculative but our study represents an important step toward a complete understanding
of signaling via GLP-1 receptor. |
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