{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nStudies of the 26S proteasome subunit PSMD7 (also known as Mov34) have revealed that its MPN (Mpr1/Pad1 N-terminal) domain adopts a fold characteristic of metalloproteases but lacks the essential metal‐coordinating residues needed for catalytic activity. Instead, this domain plays a primarily structural role by stabilizing the proteasome lid and facilitating proper assembly without directly mediating proteolysis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its structural function, PSMD7 is an integral component of the 26S proteasome complex. Its biochemical characterization has shown that it can form dimers and, depending on its posttranslational modifications (for example, phosphorylation), it exhibits differences in subcellular localization between normal and transformed cells. Such modifications suggest additional, proteasome‐independent roles including transcriptional regulation that may be critical in cellular homeostasis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPSMD7 has also emerged as a key regulator in cancer biology. In gastric cancer, PSMD7 is frequently overexpressed, and its heightened expression correlates with aggressive tumor behavior. Functional studies have demonstrated that the deubiquitinating function of PSMD7 stabilizes RAD23B and associated proteins, thereby promoting cell proliferation, migration, apoptosis resistance, and chemoresistance to agents such as cisplatin. Furthermore, its transcription can be activated by FOXP3, which in turn facilitates malignant cell growth, while similar oncogenic influences have been suggested in bladder cancer."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in proteasomal regulation and oncogenesis, PSMD7 (hVIP/mov34) is implicated in virus–host interactions. In the context of HIV-1 infection, the carboxyl-terminal region of hVIP/mov34 is essential for binding the viral accessory protein Vpr, which in turn drives the nuclear translocation of hVIP and may impact glucocorticoid receptor signaling and cell cycle regulation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn contrast to the body of work on PSMD7, another study focused on the transmembrane protein MFSD12, which functions in cysteine import into melanosomes and lysosomes and is linked to pigmentation differences among human populations. This work underscores the diversity of molecular functions uncovered in studies of related protein families."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Mathura P Ramanathan, Eugene Curley, Michael Su, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Carboxyl terminus of hVIP/mov34 is critical for HIV-1-Vpr interaction and glucocorticoid-mediated signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M203905200"}], "href": "https://doi.org/10.1074/jbc.M203905200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12237292"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12237292"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Beatriz S C Alves, Sérgio Oyama, Fábio C Gozzo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Characterization of the human ortholog of Mov34 reveals eight N-terminal residues important for MPN domain stability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2006.06.133"}], "href": "https://doi.org/10.1016/j.bbrc.2006.06.133"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16842755"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16842755"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "H Garrett R Thompson, Joseph W Harris, James P Brody "}, {"type": "b", "children": [{"type": "t", "text": "Post-translationally modified S12, absent in transformed breast epithelial cells, is not associated with the 26S proteasome and is induced by proteasome inhibitor."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Cancer (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/ijc.20261"}], "href": "https://doi.org/10.1002/ijc.20261"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15221960"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15221960"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Mario Sanches, Beatriz S C Alves, Nilson I T Zanchin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The crystal structure of the human Mov34 MPN domain reveals a metal-free dimer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.jmb.2007.04.084"}], "href": "https://doi.org/10.1016/j.jmb.2007.04.084"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17559875"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17559875"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Jianjiang Wang, Runkun Liu, Huanye Mo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deubiquitinase PSMD7 promotes the proliferation, invasion, and cisplatin resistance of gastric cancer cells by stabilizing RAD23B."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Biol Sci (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.7150/ijbs.61128"}], "href": "https://doi.org/10.7150/ijbs.61128"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34512150"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34512150"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Yujie Xu, Dingmao Wang, Guodong Zhao "}, {"type": "b", "children": [{"type": "t", "text": "Transcriptional activation of Proteasome 26S non-ATPase subunit 7 by forkhead box P3 participates in gastric cancer cell proliferation and apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Bioengineered (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/21655979.2021.2018097"}], "href": "https://doi.org/10.1080/21655979.2021.2018097"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35037550"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35037550"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Jun Wang, Tao Wang, Yuan-Kang Feng, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deubiquitinating enzyme PSMD7 promotes bladder cancer development: Involvement of RAB1A stabilization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Signal (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellsig.2023.110996"}], "href": "https://doi.org/10.1016/j.cellsig.2023.110996"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38040402"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38040402"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Dawn E Watkins-Chow, Arturo A Incao, Cecelia Rivas, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The MFSD12 p.Tyr182His common variant is sufficient to alter mouse agouti coat color."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Pigment Cell Melanoma Res (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/pcmr.13144"}], "href": "https://doi.org/10.1111/pcmr.13144"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37874775"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37874775"}]}]}]}