ZC3H11A

Last update 23 Jan 2025

Basic Info

Synonyms

KIAA0663, ZC3H11A, ZC3HDC11A

+ [2]

Introduction

RNA-binding protein that interacts with purine-rich sequences and is involved in nuclear mRNA export; probably mediated by association with the TREX complex. (Microbial infection) Plays a role in efficient growth of several nuclear-replicating viruses such as HIV-1, influenza virus or herpes simplex virus 1/HHV-1. Required for efficient viral mRNA Export.

100 Clinical Results associated with ZC3H11A

100 Translational Medicine associated with ZC3H11A

0 Patents (Medical) associated with ZC3H11A

Literatures (Medical) associated with ZC3H11A

01 Dec 2024·Molecular Therapy - Nucleic Acids

Targeting ZC3H11A elicits immunogenic cancer cell death through augmentation of antigen presentation and interferon response

Article

Author: Darweesh, Mahmoud ; Ali, Arwa ; Jin, Chuan ; Contreras, Paola ; Essand, Magnus ; Yu, Di ; Andersson, Leif

Zinc finger CCCH containing 11A (ZC3H11A) is a stress-induced protein that is upregulated in various conditions such as heat shock and virus infection. It has also been reported to be upregulated in certain cancers. The aim of this study was to evaluate the feasibility of targeting ZC3H11A as a therapeutic approach for cancer treatment, using nuclease-resistant, affinity-enhanced antisense oligonucleotide (ASO). An ASO targeting ZC3H11A was validated and evaluated in vitro and in the B16 melanoma model in vivo. Antigen presentation, interferon response, cell proliferation, and apoptosis were transcriptionally affected. These findings were validated on the protein level by the upregulation of major histocompatibility complex class I (MHC class I), an increased secretion of interferon-β (IFN-β), and induction of apoptosis observed as upregulation of caspases and annexin V. Immunogenic features of the induced apoptosis were evidenced by the surface exposure of calreticulin (CRT) and the secretion of ATP leading to enhanced dendritic cell (DC) phagocytosis, maturation, and activation. Treatment with the ZC3H11A-targeted ASO had limited efficacy in vivo, while constitutive lentiviral shRNA knockdown of ZC3H11A in murine B16 melanoma cells and human HeLa cells led to reduced tumor growth with prolonged survival of mice, validating ZC3H11A as a relevant target for cancer therapy.

01 Oct 2024·Protein Expression and Purification

Production of stable and pure ZC3H11A – An extensively disordered RNA binding protein

Article

Author: Fekry, Mostafa ; Danielson, U Helena ; Stenberg, Gun ; Dobritzsch, Doreen

Human ZC3H11A is an RNA-binding zinc finger protein involved in mRNA export and required for the efficient growth of human nuclear replicating viruses. Its biochemical properties are largely unknown so our goal has been to produce the protein in a pure and stable form suitable for its characterization. This has been challenging since the protein is large (810 amino acids) and with only the N-terminal zinc finger domain (amino acids 1-86) being well structured, the remainder is intrinsically disordered. Our production strategies have encompassed recombinant expression of full-length, truncated and mutated ZC3H11A variants with varying purification tags and fusion proteins in several expression systems, with or without co-expression of chaperones and putative interaction partners. A range of purification schemes have been explored. Initially, only truncated ZC3H11A encompassing the zinc finger domain could successfully be produced in a stable form. It required recombinant expression in insect cells since expression in E. coli gave a protein that aggregated. To reduce problematic nucleic acid contaminations, Cys8, located in one of the zinc fingers, was substituted by Ala and Ser. Interestingly, this did not affect nucleic acid binding, but the full-length protein was stabilised while the truncated version was insoluble. Ultimately, we discovered that when using alkaline buffers (pH 9) for purification, full-length ZC3H11A expressed in Sf9 insect cells was obtained in a stable and >90 % pure form, and as a mixture of monomers, dimers, tetramers and hexamers. Many of the challenges experienced are consistent with its predicted structure and unusual charge distribution.

01 Mar 2024·Journal of Biological Chemistry

Identification of RSK substrates using an analog-sensitive kinase approach

Article

Author: Lizcano-Perret, Belén ; Roux, Philippe P ; Michiels, Thomas ; Vertommen, Didier ; Gatto, Laurent ; Herinckx, Gaëtan ; Calabrese, Viviane

The p90 ribosomal S6 kinases (RSK) family of serine/threonine kinases comprises four isoforms (RSK1-4) that lie downstream of the ERK1/2 mitogen-activated protein kinase pathway. RSKs are implicated in fine tuning of cellular processes such as translation, transcription, proliferation, and motility. Previous work showed that pathogens such as Cardioviruses could hijack any of the four RSK isoforms to inhibit PKR activation or to disrupt cellular nucleocytoplasmic trafficking. In contrast, some reports suggest nonredundant functions for distinct RSK isoforms, whereas Coffin-Lowry syndrome has only been associated with mutations in the gene encoding RSK2. In this work, we used the analog-sensitive kinase strategy to ask whether the cellular substrates of distinct RSK isoforms differ. We compared the substrates of two of the most distant RSK isoforms: RSK1 and RSK4. We identified a series of potential substrates for both RSKs in cells and validated RanBP3, PDCD4, IRS2, and ZC3H11A as substrates of both RSK1 and RSK4, and SORBS2 as an RSK1 substrate. In addition, using mutagenesis and inhibitors, we confirmed analog-sensitive kinase data showing that endogenous RSKs phosphorylate TRIM33 at S1119. Our data thus identify a series of potential RSK substrates and suggest that the substrates of RSK1 and RSK4 largely overlap and that the specificity of the various RSK isoforms likely depends on their cell- or tissue-specific expression pattern.

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ZC3H11A

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