SERTAD3

Last update 08 May 2025

Basic Info

Synonyms

RBT1, Replication protein-binding trans-activator, RPA-binding trans-activator

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Introduction

Antiviral interferon-stimulated protein that plays a role in innate immunity and in the suppression of viruses through different mechanisms (PubMed:33147462, PubMed:36594413). Plays a role in the late phase response of TLR-induced immune effector expression (By similarity). During influenza infection, interacts with PB2, PB1, and PA to disrupt the formation of the viral RdRp complex (PubMed:33147462). Inhibits zika virus by interacting with the capsid protein in the nucleolus and reducing its abundance through proteasomal degradation (PubMed:36594413). Strong transcriptional coactivator (PubMed:10982866).

100 Clinical Results associated with SERTAD3

100 Translational Medicine associated with SERTAD3

0 Patents (Medical) associated with SERTAD3

Literatures (Medical) associated with SERTAD3

01 May 2025·International Journal of Biological Macromolecules

SERTAD3 interacts with porcine reproductive and respiratory syndrome virus nonstructural protein 9 and inhibits virus replication

Article

Author: He, Zhan ; Guo, Chunhe ; Wang, Jingxing ; Long, Xiaoqin ; Li, Songbei ; Chen, Yongjie

Porcine reproductive and respiratory syndrome virus (PRRSV)-encoded nonstructural protein 9 (Nsp9) has RNA-dependent RNA polymerase (RdRp) function and plays a key role in virus replication. Exploring the interaction of PRRSV Nsp9 with host proteins is important for understanding virus pathogenesis. Here, we found that the SERTA domain containing 3 (SERTAD3) is one of the host interacting factors of viral Nsp9 through yeast two-hybrid screening. The computational simulations and coimmunoprecipitation assay also confirmed their interaction. Further, SERTAD3 interacted with the nidovirus RdRp-associated nucleotidyltransferase (NiRAN) domain of Nsp9, while multiple domains of SERTAD3 interacted with Nsp9. PRRSV infection promoted SERTAD3 expression in vitro. SERTAD3 knockdown significantly facilitated PRRSV replication, while its overexpression led to a significant decrease in virus infection, demonstrating that SERTAD3 acts as a negative regulator during PRRSV replication. Mechanistically, we identified that the C-terminal activation domain of SERTAD3 was crucial for its inhibition of PRRSV. The deletion of the activation domain of SERTAD3 significantly impaired its binding ability to Nsp9, indicating that the potent interaction between its activation domain and Nsp9 is crucial for virus inhibition. This study reveals that SERTAD3 acts as a host limiting factor for PRRSV and provides a molecular basis for developing antivirals against PRRSV.

01 Apr 2025·Cell Chemical Biology

Molecular mechanism of PP2A/B55α phosphatase inhibition by IER5

Article

Author: Wang, Shumei ; Aster, Jon C ; Rawson, Shaun ; Pan, Li ; Yang, Annie ; Padi, Sathish K R ; Blacklow, Stephen C ; Cao, Ruili ; Jones, Daniel T D

PP2A serine/threonine phosphatases are heterotrimeric complexes that execute many essential physiologic functions. These activities are modulated by additional regulatory proteins, such as ARPP19, FAM122A, and IER5. Here, we report the cryoelectron microscopy (cryo-EM) structure of a complex of PP2A/B55α with the N-terminal structured region of IER5 (IER5-N50), which occludes a surface on B55α used for substrate recruitment, and show that IER5-N50 inhibits PP2A/B55α catalyzed dephosphorylation of pTau in biochemical assays. Mutations of full-length IER5 that disrupt its PP2A/B55α interface interfere with co-immunoprecipitation of PP2A/B55α. IER5 antagonism of B55α in keratinocytes is required for expression of KRT1, a differentiation marker. Mini-IER5 composed of IER5-N50 and a nuclear localization sequence restores this activity in IER5 knockout cells. Using structural bioinformatics, we identify homology of IER5-N50 with SERTA (SEI-1, RBT-1, and TARA) domain containing proteins. These studies define the molecular basis of PP2A/B55α nuclear inhibition by IER5 and suggest a roadmap for selective pharmacologic modulation of PP2A/B55α complexes.

01 Feb 2023·Journal of Medical Virology

SERTAD3 induces proteasomal degradation of ZIKV capsid protein and represents a therapeutic target

Article

Author: Cai, Qiaomei ; Nielsen‐Saines, Karin ; Cheng, Genhong ; Aliyari, Saba R. ; Qin, Cheng‐Feng ; Sun, Nina ; Song, Guang‐Yuan ; Yang, Heng ; Zhang, Rong‐Rong ; Jung, Jae U.

AbstractZika virus (ZIKV) is a mosquito‐borne RNA virus that belongs to the Flaviviridae family. While flavivirus replication is known to occur in the cytoplasm, a significant portion of the viral capsid protein localizes to the nucleus during infection. However, the role of the nuclear capsid is less clear. Herein, we demonstrated SERTA domain containing 3 (SERTAD3) as an antiviral interferon stimulatory gene product had an antiviral ability to ZIKV but not JEV. Mechanistically, we found that SERTAD3 interacted with the capsid protein of ZIKV in the nucleolus and reduced capsid protein abundance through proteasomal degradation. Furthermore, an eight amino acid peptide of SERTAD3 was identified as the minimum motif that binds with ZIKV capsid protein. Remarkably, the eight amino acids synthetic peptide from SERTAD3 significantly prevented ZIKV infection in culture and pregnant mouse models. Taken together, these findings not only reveal the function of SERTAD3 in promoting proteasomal degradation of a specific viral protein but also provide a promising host‐targeted therapeutic strategy against ZIKV infection.

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SERTAD3

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