Interferon-induced PARP14-mediated ADP-ribosylation in p62 bodies requires the ubiquitin-proteasome system DOI Creative Commons
Rameez Raja, Banhi Biswas, Rachy Abraham

и другие.

The EMBO Journal, Год журнала: 2025, Номер unknown

Опубликована: Апрель 7, 2025

Abstract Biomolecular condensates are cellular compartments without enveloping membranes, enabling them to dynamically adjust their composition in response environmental changes through post-translational modifications. Recent work has revealed that interferon-induced ADP-ribosylation (ADPr), which can be reversed by a SARS-CoV-2-encoded hydrolase, is enriched within condensate. However, the identity of condensate and responsible host ADP-ribosyltransferase remain elusive. Here, we demonstrate interferon induces ADPr transcriptional activation PARP14, requiring both physical presence catalytic activity PARP14 for formation. Interferon-induced colocalizes with its associated E3 ligase, DTX3L. These PARP14/ADPr contain key components p62 bodies—including selective autophagy receptor p62, binding partner NBR1 protein TAX1BP1, along K48-linked K63-linked polyubiquitin chains—but lack autophagosome marker LC3B. Knockdown disrupts formation these condensates. Importantly, structures unaffected inhibition, but depend on ubiquitination proteasome activity. Taken together, findings triggers PARP14-mediated bodies, requires an active ubiquitin-proteasome system.

Язык: Английский

Interferon-induced PARP14-mediated ADP-ribosylation in p62 bodies requires the ubiquitin-proteasome system DOI Creative Commons
Rameez Raja, Banhi Biswas, Rachy Abraham

и другие.

The EMBO Journal, Год журнала: 2025, Номер unknown

Опубликована: Апрель 7, 2025

Abstract Biomolecular condensates are cellular compartments without enveloping membranes, enabling them to dynamically adjust their composition in response environmental changes through post-translational modifications. Recent work has revealed that interferon-induced ADP-ribosylation (ADPr), which can be reversed by a SARS-CoV-2-encoded hydrolase, is enriched within condensate. However, the identity of condensate and responsible host ADP-ribosyltransferase remain elusive. Here, we demonstrate interferon induces ADPr transcriptional activation PARP14, requiring both physical presence catalytic activity PARP14 for formation. Interferon-induced colocalizes with its associated E3 ligase, DTX3L. These PARP14/ADPr contain key components p62 bodies—including selective autophagy receptor p62, binding partner NBR1 protein TAX1BP1, along K48-linked K63-linked polyubiquitin chains—but lack autophagosome marker LC3B. Knockdown disrupts formation these condensates. Importantly, structures unaffected inhibition, but depend on ubiquitination proteasome activity. Taken together, findings triggers PARP14-mediated bodies, requires an active ubiquitin-proteasome system.

Язык: Английский

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