Mouse polyclonal to ZNF622, Host Mouse
- Known as:
- Mouse pab ZNF622, Host Mouse
- Catalog number:
- YF-PA26774
- Product Quantity:
- 50 uL
- Category:
- -
- Supplier:
- Abfron
- Gene target:
- Mouse polyclonal ZNF622 Host
Related genes to: Mouse polyclonal to ZNF622, Host Mouse
- Gene:
- ZNF622 NIH gene
- Name:
- zinc finger protein 622
- Previous symbol:
- -
- Synonyms:
- MGC2485, MGC17552, ZPR9
- Chromosome:
- 5p15.1
- Locus Type:
- gene with protein product
- Date approved:
- 2004-04-19
- Date modifiied:
- 2014-11-18
Related products to: Mouse polyclonal to ZNF622, Host Mouse
Related articles to: Mouse polyclonal to ZNF622, Host Mouse
- The correct assembly of ribosomes is essential for viability and faithful gene expression. In eukaryotic cells, the pre-40S and pre-60S ribosomal subunits are largely pre-assembled in the nucleolus before they are exported to the cytoplasm for final maturation. Although most ribosomal proteins of the large subunit are loaded onto pre-60S particles in the early nucleolar steps, a few, including eL24, are loaded in the cytoplasm. eL24 is thought to recruit the zinc-finger protein Rei1 (ZNF622 in humans). In yeast, Rei1 has a paralog, Reh1. While we and others have previously shown that Rei1 facilitates the removal of Arx1, Rei1 and Reh1 appear to have an additional unknown function. To identify this function, we first examined the protein composition of pre-60S subunits isolated from rei1Δ reh1Δ mutant cells and found that these subunits were specifically defective for eL24. However, the absence of eL24 did not impair Rei1 binding to pre-60S. Moreover, overexpression of eL24 suppressed the growth defect of the double mutant. As an alternative approach to understanding the function of Rei1 and Reh1, we screened for bypass suppressors of the growth defect of rei1Δ reh1Δ cells. We identified mutations in the genes coding for ribosomal protein uL3, the GTPase Lsg1 and the protein phosphatase Ppq1. Importantly, these suppressors all partially reversed the eL24 loading defect of rei1Δ reh1Δ cells. Based on these results, we propose a revised order of cytoplasmic assembly events where Rei1 and Reh1 facilitate the recruitment of eL24 to the pre-60S particle. - Source: PubMed
Publication date: 2026/08/19
Lin RanReynolds Madison JShankar Nila RJohnson Arlen W - The correct assembly of ribosomes is essential for viability and faithful gene expression. In eukaryotic cells, the pre-40S and pre-60S ribosomal subunits are largely pre-assembled in the nucleolus before they are exported to the cytoplasm for final maturation. Although most ribosomal proteins of the large subunit are loaded onto pre-60S particles in the early nucleolar steps, a few, including eL24, are loaded in the cytoplasm. eL24 is thought to recruit the zinc-finger protein Rei1 (ZNF622 in humans). In yeast, Rei1 has a paralog, Reh1. While we and others have previously shown that Rei1 facilitates the removal of Arx1, Rei1 and Reh1 appear to have an additional unknown function. To identify this function, we first examined the protein composition of pre-60S subunits isolated from mutant cells and found that these subunits were specifically defective for eL24. However, the absence of eL24 did not impair Rei1 binding to pre-60S. Moreover, overexpression of eL24 suppressed the growth defect of the double mutant. As an alternative approach to understanding the function of Rei1 and Reh1, we screened for bypass suppressors of the growth defect of cells. We identified mutations in the genes coding for ribosomal protein uL3, the GTPase Lsg1 and the protein phosphatase Ppq1. Importantly, these suppressors all partially reversed the eL24 loading defect of cells. Based on these results, we propose a revised order of cytoplasmic assembly events where Rei1 and Reh1 facilitate the recruitment of eL24 to the pre-60S particle. - Source: PubMed
Publication date: 2026/04/02
Lin RanReynolds Madison JShankar Nila RJohnson Arlen W - Protein phosphatases are critical for regulating cell signaling, cell cycle, and cell fate decisions, and their dysregulation leads to an array of human diseases like cancer. The dual specificity phosphatases (DUSPs) have emerged as important factors driving tumorigenesis and cancer therapy resistance. DUSP12 is a poorly characterized atypical DUSP widely conserved throughout evolution. Although no direct substrate has been firmly established, DUSP12 has been implicated in protecting cells from stress, regulating ribosomal biogenesis, and modulating cellular DNA content. In this study, we used affinity- and proximity-based biochemical purification approaches coupled to mass spectrometry to identify the zinc finger protein ZNF622 as a novel DUSP12 interactor, which was validated by in cell and in vitro IP assays. Interestingly, ZNF622 binds to the unique zinc-binding domain of DUSP12, which previous reports indicated was important for many of DUSP12's functions within the cell. Prior studies had implicated ZNF622 as a modulator of apoptosis, but it remained unclear if and how ZNF622 participated in the cell cycle and, more so, how it promoted cell death. Using mass spectrometry analyses, we found that overexpression of DUSP12 promoted de-phosphorylation of ZNF622 at Ser. Overexpression of ZNF622, but not Ser phosphomimetic and phosphorylation-deficient mutants, led to an increase in pre-metaphase mitotic defects while knockdown of DUSP12 also showed mitotic defects in metaphase. Furthermore, knockdown of DUSP12 promoted, while knockdown of ZNF622 suppressed, stress-induced apoptosis. Our results support a model where DUSP12 protects cells from ZNF622 mediated stress-induced apoptosis. - Source: PubMed
Publication date: 2026/03/18
Abdusamad MaiGuo XiaoRamirez IvanVelasquez Erick FCohn WhitakerGholkar Ankur AAshley Immy ADelgado YenniferBouhaddou MehdiWhitelegge Julian PDamoiseaux RobertTorres Jorge Z - Plasticity in teleosts is a fascinating evolutionary strategy enables species to acclimate to environmental changes. However, the molecular mechanisms that underlie gonadal differentiation and reversal remain incompletely understood. The four-finger threadfin (Eleutheronema tetradactylum), a protandrous hermaphrodite belonging to the Polynemidae family, serves as an excellent model for studying genes and molecules involved in gonadal transformation. In this study, we used de novo transcriptome sequencing of the male and female gonads to identify key regulatory genes and pathways involved in sex differentiation. A total of 12,034 DEGs were identified, with 7567 upregulated and 4467 downregulated between testes and ovaries. GO and KEGG enrichment analyses identified steroid hormone biosynthesis as the key pathway in gonadal differentiation. Several novel sex biased genes DEGs were identified, including testis-biased genes nefl, rfesd, and gpatch8, and ovary-biased genes ift57, hoxb5a, naxd, and tgfbr3. furthermore, clusters of testis-specific genes, including dnah7, tspan1, hspa8, dnah3, dnah6, dnah17, myo10, kcnq3, dnaaf11, rtase, dmrt1, smcl1b, slc44a5b, tex11,cyp51 and ovary-biased genes, such as cd9, zp2, ccnp, cldnd, znf622, tc1a, hsd17b7, foxl2, sox3, and sox19a were identified, emphasizing their crucial roles in gonadal differentiation. This in-depth transcriptomic study sheds light on the molecular foundations of reproductive adaptability, offering novel insights for disciplines such as aquaculture, conservation and evolutionary biology. - Source: PubMed
Publication date: 2025/07/21
Mkulo Evodia MosesIddrisu LukmanIbrahim SalifuHuang JianshengWang LinjuanZheng AnnaMwemi Happiness MosesMinxuan JinZhang HuijuanTang BaoguiMa QianAmoah KwakuWang BeiWang Zhongliang - Protein phosphatases are critical for regulating cell signaling, cell cycle, and cell fate decisions, and their dysregulation leads to an array of human diseases like cancer. The dual specificity phosphatases (DUSPs) have emerged as important factors driving tumorigenesis and cancer therapy resistance. DUSP12 is a poorly characterized atypical DUSP widely conserved throughout evolution. Although no direct substrate has been firmly established, DUSP12 that has been implicated in protecting cells from stress, regulating ribosomal biogenesis, and modulating cellular DNA content. In this study, we used affinity- and proximity-based biochemical purification approaches coupled to mass spectrometry to identify the zinc finger protein ZPR9 as a novel DUSP12 interactor, which was validated by in-cell and IP assays. Interestingly, ZPR9 binds to the unique zinc-binding domain of DUSP12, which previous reports indicated was important for many of DUSP12's functions within the cell. Prior studies had implicated ZPR9 as a modulator of apoptosis, but it remained unclear if and how ZPR9 participated in the cell cycle and, more so, how it promoted cell death. Using mass spectrometry analyses, we found that overexpression of DUSP12 promoted de-phosphorylation of ZPR9 at Ser. Overexpression of ZPR9, but not Ser phosphomimetic and phosphorylation-deficient mutants, led to an increase in pre-metaphase mitotic defects while knockdown of DUSP12 also showed mitotic defects in metaphase. Furthermore, knockdown of DUSP12 promoted, while knockdown of ZPR9 suppressed, stress-induced apoptosis. Our results support a model where DUSP12 protects cells from stress-induced apoptosis by promoting de-phosphorylation of ZPR9. - Source: PubMed
Publication date: 2025/01/14
Abdusamad MaiGuo XiaoRamirez IvanVelasquez Erick FCohn WhitakerGholkar Ankur AWhitelegge Julian PTorres Jorge Z