SERTAD1 antibody - N-terminal region (ARP34309_P050)
- Known as:
- SERTAD1 (anti-) - N-terminal region (ARP34309_P050)
- Catalog number:
- arp34309_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- SERTAD1 antibody - N-terminal region (ARP34309_P050)
Related genes to: SERTAD1 antibody - N-terminal region (ARP34309_P050)
- Gene:
- SERTAD1 NIH gene
- Name:
- SERTA domain containing 1
- Previous symbol:
- -
- Synonyms:
- SEI1, TRIP-Br1
- Chromosome:
- 19q13.1-q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2004-02-16
- Date modifiied:
- 2014-11-19
Related products to: SERTAD1 antibody - N-terminal region (ARP34309_P050)
Related articles to: SERTAD1 antibody - N-terminal region (ARP34309_P050)
- - Source: PubMed
Publication date: 2026/03/07
Hu ChangyanMiao JuanjuanZhao QihongChen Lijian - Aberrant activation of autophagy contributes to neuronal cell death and plays a pivotal role in the pathogenesis of Alzheimer's disease (AD). To study this further, we assessed autophagy-related (ATG) proteins in 5xFAD mice at different ages and found a progressive inappropriate elevation of autophagic proteins in these mice. We identified a transcriptional coregulator, Sertad1 (SERTA domain-containing protein 1), which plays a necessary role in neuron death, as a key regulator of aberrant autophagy in AD. We found a progressive elevation in Sertad1 levels in 5xFAD mice with age compared with WT mice. Sertad1 knockdown in 5xFAD mice brains lowered levels of ATG proteins and lysosomal proteins, suggesting its role in the regulation of the autophagy-lysosomal pathway. We found that Sertad1 knockdown restored Akt activity, which is inhibited in AD, and blocked the activation of its target, FoxO3a, which is translocated to the nucleus in the absence of active Akt and mediates neuron death by apoptosis and autophagy. Furthermore, we showed that lentivirus-mediated RNAi targeting of Sertad1 in 5xFAD mice led to better performance in behavioral experiments compared with 5xFAD mice treated with nontargeting shRNA, accompanied by significant restoration of synaptic integrity. Overall, our results demonstrated that autophagy is robustly induced with disease progression, but ATG proteins accumulate in the brain because of their impaired clearance; Sertad1 knockdown restored synaptic failure and improved cognition in 5xFAD mice by enhancing clearance of ATG proteins and neuronal survival. Hence, Sertad1 could be an excellent target for therapeutic intervention to combat the multifaceted pathologies of AD. - Source: PubMed
Publication date: 2025/10/29
Ambareen NaqiyaGharami KusumikaMondal AnanyaSarkar Uday AdityaBiswas Subhas C - Cell division cycle-associated protein 4 (CDCA4) has the potential to indicate lung adenocarcinoma (LUAD) development, but its regulatory role in mitophagy remains unclear. This study aimed to elucidate the mitophagy regulation and therapeutic implications of CDCA4 in LUAD. CDCA4 expression was significantly elevated in LUAD clinical specimens versus paracancerous tissues and inversely correlated with mitophagy activity. Lentiviral vectors were employed to manipulate established LUAD cells, followed by treatment with chloroquine (CQ; lysosomal inhibitor) and rapamycin (autophagy inducer) in CDCA4-silenced cells. CDCA4 knockdown elevated total and mitochondrial superoxide levels, disrupted mitochondrial membrane potential, activated the PINK1/Parkin pathway, enhanced LC3-II conversion, and degraded mitochondrial membrane proteins, collectively promoting mitophagy. Silencing CDCA4 suppressed malignant phenotypes (proliferation/migration), effects reversed by CQ but exacerbated by rapamycin. Mechanistically, CDCA4 interacted with SERTAD1 and E2F1 and stabilized these proteins. The promotion of mitophagy by CDCA4 silencing was impaired by the overexpression of SERTAD1 and E2F1. LUAD cells silencing CDCA4 were injected into immunodeficient mice for in vivo verification. CDCA4-silenced xenografts exhibited suppressed tumor growth, increased apoptosis, and elevated mitophagy-related markers. This study identifies the CDCA4/SERTAD1/E2F1 complex as a pivotal mitophagy-inhibitory hub in LUAD, proposing this axis as a novel predictive and therapeutic target. - Source: PubMed
Tan JianlongWang JufenZhang WeidongZhang Cuihua - The activity of protein phosphatase 2A containing the B55 regulatory subunit (PP2A:B55) is tightly controlled by various positive and negative modulators. IER family proteins function as adapters by simultaneously binding the B55 subunit and specific substrates, thereby promoting their dephosphorylation by PP2A:B55. Here, we report that the B55-binding domain of IER proteins shares significant amino acid homology with the SERTA domain of the SERTAD family. All SERTAD family members-SERTAD1, SERTAD2, SERTAD3, SERTAD4, and CDCA4-bind to B55-containing PP2A complexes. Among these, SERTAD1 induces dephosphorylation of heat shock factor HSF1 at Ser320, leading to suppression of HSF1 transcriptional activity. This regulatory function of SERTAD1 requires its nuclear localization and interaction with both HSF1 and the B55 subunit. In contrast, the PP2A:B55 adapter IER5 promotes dephosphorylation of HSF1 at Ser303, Ser307, and Ser320, resulting in enhanced HSF1 activity. The differential dephosphorylation patterns mediated by SERTAD1 and IER5 are attributed to structural differences in helix 1 of their respective B55-binding domains. These findings identify SERTAD1 as a novel PP2A:B55 adapter and highlight the role of the B55-binding domain in governing site-specific substrate dephosphorylation. - Source: PubMed
Publication date: 2025/09/24
Sugiyama HarukaNakada TaiseiYano KoyoSakurai Hiroshi - The ubiquitin chains perform diverse biological functions through different linkages. However, the understanding of non-canonical K29-linked ubiquitin chains is relatively limited. Exploring the physiological functions of K29-linked ubiquitin chains beyond degradation is crucial for deciphering the ubiquitin chain code, which is essential for understanding cellular physiology. The unfolded protein response (UPR) serves as a crucial mechanism for cells to cope with endoplasmic reticulum stress and involves comprehensive and precise regulation. Ubiquitin, as a regulator of protein function, has potential regulatory functions other than guiding protein degradation in the UPR. Here, a close association is revealed between K29-linked ubiquitin chains and transcriptional regulation during the UPR. After UPR induction, the K29-linked ubiquitination of the SMC1A and SMC3 proteins in the cohesin complex increases. The transcription of cell proliferation-related genes, such as SERTAD1 and NUDT16L1, is regulated by the K29-linked ubiquitination of cohesin. Overall, the upregulation of K29-linked ubiquitination of cohesin during the UPR disrupts the formation of the transcription initiation complex, resulting in the transcriptional downregulation of cell proliferation-related genes. - Source: PubMed
Publication date: 2025/08/30
Zhang QiushuangTeng XucongDai YicongWu YuncongHou HongweiLi Jinghong