CACTIN

Last update 08 May 2025

Basic Info

Synonyms

C19orf29, CACTIN, cactin, spliceosome C complex subunit

+ [3]

Introduction

Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (PubMed:28062851). Required for the splicing of CDCA5/Sororin, a regulator of sister chromatid cohesion (PubMed:28062851). Involved in the regulation of innate immune response (PubMed:20829348). Acts as a negative regulator of Toll-like receptor, interferon-regulatory factor (IRF) and canonical NF-kappa-B signaling pathways (PubMed:20829348, PubMed:26363554). Contributes to the regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous pro-inflammatory stimuli (PubMed:20829348, PubMed:26363554).

100 Clinical Results associated with CACTIN

100 Translational Medicine associated with CACTIN

0 Patents (Medical) associated with CACTIN

Literatures (Medical) associated with CACTIN

01 Dec 2024·Plant Cell Reports

OsCactin positively regulates the drought stress response in rice

Article

Author: Wang, Mingyue ; Li, Zhihui ; Zhang, Zhihong ; Jiang, Shan ; Zhu, Menghao ; Chu, Zhaohui ; Zhu, Mingqiang ; Huang, Wenchao ; Xu, Shuang ; Huang, Jinqiu

KEY MESSAGEOsCactinpositively regulates drought tolerance in rice. OsCactin is regulated by OsTRAB1 and interacts with OsDi19 proteins to defend against drought stress. Drought stress significantly limits plant growth and production. Cactin, a CactinC_cactus domain-containing protein encoded by a highly conserved single-copy gene prevalent across the eukaryotic kingdom, is known to play diverse roles in fundamental biological processes. However, its function in rice drought tolerance remains poorly understood. In this study, with its overexpression and knockout rice lines in both a pot drought experiment and a PEG drought-simulation test, OsCactin was found to positively regulate rice drought tolerance during the rice seedling stage. The OsCactin-overexpressing lines presented high tolerance to drought stress, whereas the OsCactin-knockout plants were sensitive to drought stress. OsCactin was localized in the nucleus, and was predominantly expressed in the leaves and panicles at the seedling and booting stages, respectively. Furthermore, OsTRAB1, a drought-responsive TF of the bZIP family, binds to the promoter of OsCactin as a drought-responsive regulator. OsDi19 proteins, the Cys2/His2 (C2H2)-type zinc finger TFs from the drought-induced 19 family, interact with OsCactin both in vitro and in vivo. Our results provide new insights into the intricate mechanisms by which OsCactin regulates the rice drought stress response, which may contribute to the design of molecular breeding methods for rice.

30 Oct 2024·Journal of Experimental Botany

SCI1, a flower regulator of cell proliferation, and its partners NtCDKG2 and NtRH35 interact with the splicing machinery

Article

Author: Strini, Edward J ; Aziani, Rodrigo ; Quiapim, Andréa C ; Pinoti, Vitor F ; Ferreira, Pedro B ; Pranchevicius, Maria Cristina S ; Araujo, Ana Paula U ; Cruz, Joelma O ; Goldman, Maria Helena S ; Thomé, Vanessa ; De Paoli, Henrique C ; Pinto, Andressa P A ; Lubini, Greice

AbstractSuccessful plant reproduction depends on the adequate development of floral organs controlled by cell proliferation and other processes. The Stigma/style cell-cycle inhibitor 1 (SCI1) gene regulates cell proliferation and affects the final size of the female reproductive organ. To unravel the molecular mechanism exerted by Nicotiana tabacum SCI1 in cell proliferation control, we searched for its interaction partners through semi-in vivo pull-down experiments, uncovering a cyclin-dependent kinase, NtCDKG;2. Bimolecular fluorescence complementation and co-localization experiments showed that SCI1 interacts with NtCDKG;2 and its cognate NtCyclin L in nucleoli and splicing speckles. The screening of a yeast two-hybrid cDNA library using SCI1 as bait revealed a novel DEAD-box RNA helicase (NtRH35). Interaction between the NtCDKG;2–NtCyclin L complex and NtRH35 is also shown. Subcellular localization experiments showed that SCI1, NtRH35, and the NtCDKG;2–NtCyclin L complex associate with each other within splicing speckles. The yeast two-hybrid screening of NtCDKG;2 and NtRH35 identified the conserved spliceosome components U2aʹ, NF-κB activating protein (NKAP), and CACTIN. This work presents SCI1 and its interactors, the NtCDKG;2–NtCyclin L complex and NtRH35, as new spliceosome-associated proteins. Our findings reveal a network of interactions and indicate that SCI1 may regulate cell proliferation through the splicing process, providing new insights into the intricate molecular pathways governing plant development.

14 May 2024·Journal of Virology

Regulation of ubiquitination and antiviral activity of Cactin by deubiquitinase Usp14 in Drosophila

Article

Author: Xu, Wen ; Zhang, Liqin ; Rong, Qiqi ; Wu, Qingfa ; Xi, Zhichong ; Guo, Dongyang

ABSTRACT Cactin, a highly conserved protein, plays a crucial role in various physiological processes in eukaryotes, including innate immunity. Recently, the function of Cactin in the innate immunity of Drosophila has been explored, revealing that Cactin regulates a non-canonical signaling pathway associated with the Toll and Imd pathways via the Cactin-Deaf1 axis. In addition, Cactin exhibits specific antiviral activity against the Drosophila C virus (DCV) in Drosophila , with an unknown mechanism. During DCV infection, it has been confirmed that the protein level and antiviral activity of Cactin are regulated by ubiquitination. However, the precise ubiquitination and deubiquitination mechanisms of Cactin in Drosophila remain unexplored. In this study, we identified ubiquitin-specific protease 14 (Usp14) as a major deubiquitinase for Cactin through comprehensive deubiquitinase screening. Our results demonstrate that Usp14 interacts with the C_Cactus domain of Cactin via its USP domain. Usp14 efficiently removes K48- and K63-linked polyubiquitin chains from Cactin, thereby preventing its degradation through the ubiquitin-proteasome pathway. Usp14 significantly inhibits DCV replication in Drosophila cells by stabilizing Cactin. Moreover, Usp14-deficient fruit flies exhibit increased susceptibility to DCV infection compared to wild-type flies. Collectively, our findings reveal the regulation of ubiquitination and antiviral activity of Cactin by the deubiquitinase Usp14, providing valuable insights into the modulation of Cactin-mediated antiviral activity in Drosophila . IMPORTANCE Viral infections pose a severe threat to human health, marked by high pathogenicity and mortality rates. Innate antiviral pathways, such as Toll, Imd, and JAK-STAT, are generally conserved across insects and mammals. Recently, the multi-functionality of Cactin in innate immunity has been identified in Drosophila . In addition to regulating a non-canonical signaling pathway through the Cactin-Deaf1 axis, Cactin exhibits specialized antiviral activity against the Drosophila C virus (DCV) with an unknown mechanism. A previous study emphasized the significance of the Cactin level, regulated by the ubiquitin-proteasome pathway, in modulating antiviral signaling. However, the regulatory mechanisms governing Cactin remain unexplored. In this study, we demonstrate that Usp14 stabilizes Cactin by preventing its ubiquitination and subsequent degradation. Furthermore, Usp14 plays a crucial role in regulating the antiviral function mediated by Cactin. Therefore, our findings elucidate the regulatory mechanism of Cactin in Drosophila , offering a potential target for the prevention and treatment of viral infections.

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CACTIN

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