4abl
HUMAN PARP14 (ARTD8, BAL2) - MACRO DOMAIN 3HUMAN PARP14 (ARTD8, BAL2) - MACRO DOMAIN 3
Structural highlights
FunctionPAR14_HUMAN Enhances STAT6-dependent transcription (By similarity). Has ADP-ribosyltransferase activity. Publication Abstract from PubMedADP-ribosyltransferases (ARTs) catalyze the transfer of ADP-ribose from NAD onto substrates. Some ARTs generate in an iterative process ADP-ribose polymers that serve as adaptors for distinct protein domains. Other ARTs, exemplified by ARTD10, function as mono-ADP-ribosyltransferases, but it has been unclear whether this modification occurs in cells and how it is read. We observed that ARTD10 colocalized with ARTD8 and defined its macrodomains 2 and 3 as readers of mono-ADP-ribosylation both in vitro and in cells. The crystal structures of these two ARTD8 macrodomains and isothermal titration calorimetry confirmed their interaction with ADP-ribose. These macrodomains recognized mono-ADP-ribosylated ARTD10, but not poly-ADP-ribosylated ARTD1. This distinguished them from the macrodomain of macroH2A1.1, which interacted with poly- but not mono-ADP-ribosylated substrates. Moreover, Ran, an ARTD10 substrate, was also read by ARTD8 macrodomains. This identifies readers of mono-ADP-ribosylated proteins, defines their structures, and demonstrates the presence of this modification in cells. Recognition of Mono-ADP-Ribosylated ARTD10 Substrates by ARTD8 Macrodomains.,Forst AH, Karlberg T, Herzog N, Thorsell AG, Gross A, Feijs KL, Verheugd P, Kursula P, Nijmeijer B, Kremmer E, Kleine H, Ladurner AG, Schuler H, Luscher B Structure. 2013 Mar 5;21(3):462-75. doi: 10.1016/j.str.2012.12.019. PMID:23473667[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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