<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Yao D</submitter><funding>Texas AgriLife Research</funding><funding>NIGMS NIH HHS</funding><funding>National Science Foundation</funding><pagination>2088-2103</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9070964</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>14(12)</volume><pubmed_abstract>Poly(ADP-ribosyl)ation (PARylation) is a posttranslational modification reversibly catalyzed by poly(ADP-ribose) polymerases (PARPs) and poly(ADP-ribose) glycohydrolases (PARGs) and plays a key role in multiple cellular processes. The molecular mechanisms by which PARylation regulates innate immunity remain largely unknown in eukaryotes. Here we show that Arabidopsis UBC13A and UBC13B, the major drivers of lysine 63 (K63)-linked polyubiquitination, directly interact with PARPs/PARGs. Activation of pathogen-associated molecular pattern (PAMP)-triggered immunity promotes these interactions and enhances PARylation of UBC13. Both parp1 parp2 and ubc13a ubc13b mutants are compromised in immune responses with increased accumulation of total pathogenesis-related (PR) proteins but decreased accumu</pubmed_abstract><journal>Molecular plant</journal><pubmed_title>Coordinated regulation of plant immunity by poly(ADP-ribosyl)ation and K63-linked ubiquitination.</pubmed_title><pmcid>PMC9070964</pmcid><funding_grant_id>R01 GM092893</funding_grant_id><funding_grant_id>IOS-1951094</funding_grant_id><pubmed_authors>Bent AF</pubmed_authors><pubmed_authors>Arguez MA</pubmed_authors><pubmed_authors>Yao D</pubmed_authors><pubmed_authors>Song J</pubmed_authors><pubmed_authors>He P</pubmed_authors></additional><is_claimable>false</is_claimable><name>Coordinated regulation of plant immunity by poly(ADP-ribosyl)ation and K63-linked ubiquitination.</name><description>Poly(ADP-ribosyl)ation (PARylation) is a posttranslational modification reversibly catalyzed by poly(ADP-ribose) polymerases (PARPs) and poly(ADP-ribose) glycohydrolases (PARGs) and plays a key role in multiple cellular processes. The molecular mechanisms by which PARylation regulates innate immunity remain largely unknown in eukaryotes. Here we show that Arabidopsis UBC13A and UBC13B, the major drivers of lysine 63 (K63)-linked polyubiquitination, directly interact with PARPs/PARGs. Activation of pathogen-associated molecular pattern (PAMP)-triggered immunity promotes these interactions and enhances PARylation of UBC13. Both parp1 parp2 and ubc13a ubc13b mutants are compromised in immune responses with increased accumulation of total pathogenesis-related (PR) proteins but decreased accumu</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Dec</publication><modification>2025-04-05T15:58:37.717Z</modification><creation>2025-04-05T15:58:37.717Z</creation></dates><accession>S-EPMC9070964</accession><cross_references><pubmed>34418551</pubmed><doi>10.1016/j.molp.2021.08.013</doi></cross_references></HashMap>