{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSTK38 (also known as NDR1) acts as a key mediator of apoptosis. In response to death receptor stimulation (by Fas and TNF‑α), STK38 becomes phosphorylated via upstream effectors including MST1 and the tumor suppressor RASSF1A, thereby promoting programmed cell death. In addition, binding partners such as MICAL‑1 can antagonize MST1-induced STK38 activation, providing a mechanism to fine‑tune apoptotic signaling."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThe catalytic activity of STK38 is governed by dynamic protein–protein interactions. Binding of human MOB1 relieves an inherent auto‑inhibitory activation segment within the kinase domain, thus potentiating STK38’s activity; in contrast, MOB2 interacts in a distinct manner to limit kinase activation. Differential subcellular distribution—illustrated by the distinct nuclear localization of STK38 versus the predominantly cytoplasmic STK2 paralogue—further refines its signaling specificity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "3", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSTK38 also plays integral roles in cell cycle regulation and mitosis. In the G1 phase, activation of STK38 by MST3 leads to the phosphorylation of cell cycle inhibitors such as p21, thereby facilitating the G1‑to‑S phase transition. During mitosis, STK38 ensures proper centrosome duplication, accurate chromosome alignment, and spindle orientation through its interactions with regulators like cyclin D1/Cdk4, CDC25A, and PLK1‑mediated phosphorylation events."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its roles in growth and division, STK38 is pivotal in cellular stress responses by regulating autophagy. It promotes autophagosome formation via interaction with key autophagic regulators such as Beclin1 and aids in the removal of damaged mitochondria (mitophagy) in response to oncogenic Ras signaling. STK38 is also activated by oxidative stress—a process modulated by AKT and restrained by GSK‑3β—and contributes to the repair of lysosomal membranes (microlysophagy) by phosphorylating scaffolds that recruit essential disassembly factors."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "14", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSTK38 dynamically shuttles between the nucleus and the cytoplasm to regulate the distribution of critical signaling molecules. By directly phosphorylating the major nuclear export receptor XPO1 on serine 1055, STK38 facilitates the nuclear exit of itself as well as other effectors such as Beclin1 and YAP1. This ability to control nuclear export underscores a broader role for STK38 in coordinating cellular responses by determining the subcellular localization of diverse proteins."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSTK38 contributes to immune and inflammatory signaling. It modulates NF‑κB activation downstream of TNF‑α via interactions with TRAF2, with its kinase activity being critical for this process. Furthermore, STK38 enhances antiviral responses by promoting type I interferon production; it does so by augmenting STAT1 translation through direct binding to regulatory regions of miR146a, thereby relieving miR146a‑mediated translational inhibition."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThe dysregulation of STK38 is implicated in a number of pathological contexts. In various cancers, altered STK38 activity drives oncogenic transformation—for instance, by modulating MEKK2 stability in gastric cancer, stabilizing MYC in lymphomas, and affecting breast cancer stem cell properties. STK38 is also involved in viral pathogenesis, being incorporated into HIV‑1 particles and processed by viral protease. Moreover, pan‑cancer analyses have identified correlations between STK38 expression and immune cell infiltration, while its interaction with PPARγ enhances protein stability to promote adipogenesis, highlighting its diverse roles in tumorigenesis, infection, and metabolic differentiation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "30"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Anton Vichalkovski, Ekaterina Gresko, Hauke Cornils, et al. "}, {"type": "b", "children": [{"type": "t", "text": "NDR kinase is activated by RASSF1A/MST1 in response to Fas receptor stimulation and promotes apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Curr Biol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cub.2008.10.060"}], "href": "https://doi.org/10.1016/j.cub.2008.10.060"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19062280"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19062280"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Yeping Zhou, Youri Adolfs, W W M Pim Pijnappel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "MICAL-1 is a negative regulator of MST-NDR kinase signaling and apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.01389-10"}], "href": "https://doi.org/10.1128/MCB.01389-10"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21730291"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21730291"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Samuel J Bichsel, Rastislav Tamaskovic, Mario R Stegert, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mechanism of activation of NDR (nuclear Dbf2-related) protein kinase by the hMOB1 protein."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M404542200"}], "href": "https://doi.org/10.1074/jbc.M404542200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15197186"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15197186"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Alexander Hergovich, Samuel J Bichsel, Brian A Hemmings "}, {"type": "b", "children": [{"type": "t", "text": "Human NDR kinases are rapidly activated by MOB proteins through recruitment to the plasma membrane and phosphorylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.25.18.8259-8272.2005"}], "href": "https://doi.org/10.1128/MCB.25.18.8259-8272.2005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16135814"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16135814"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "S Hirabayashi, K Nakagawa, K Sumita, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Threonine 74 of MOB1 is a putative key phosphorylation site by MST2 to form the scaffold to activate nuclear Dbf2-related kinase 1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2008.66"}], "href": "https://doi.org/10.1038/onc.2008.66"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18362890"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18362890"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Eric Devroe, Hediye Erdjument-Bromage, Paul Tempst, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human Mob proteins regulate the NDR1 and NDR2 serine-threonine kinases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M401999200"}], "href": "https://doi.org/10.1074/jbc.M401999200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15067004"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15067004"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Reto S Kohler, Debora Schmitz, Hauke Cornils, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Differential NDR/LATS interactions with the human MOB family reveal a negative role for human MOB2 in the regulation of human NDR kinases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.00150-10"}], "href": "https://doi.org/10.1128/MCB.00150-10"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20624913"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20624913"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Hauke Cornils, Reto S Kohler, Alexander Hergovich, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Human NDR kinases control G(1)/S cell cycle transition by directly regulating p21 stability."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.01216-10"}], "href": "https://doi.org/10.1128/MCB.01216-10"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21262772"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21262772"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Alexander Hergovich, Stefan Lamla, Erich A Nigg, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Centrosome-associated NDR kinase regulates centrosome duplication."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2007.01.020"}], "href": "https://doi.org/10.1016/j.molcel.2007.01.020"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17317633"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17317633"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Shuhei Chiba, Masanori Ikeda, Kokichi Katsunuma, et al. "}, {"type": "b", "children": [{"type": "t", "text": "MST2- and Furry-mediated activation of NDR1 kinase is critical for precise alignment of mitotic chromosomes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Curr Biol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cub.2009.02.054"}], "href": "https://doi.org/10.1016/j.cub.2009.02.054"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19327996"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19327996"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Zhaoyang Du, Xiaomei Tong, Xin Ye "}, {"type": "b", "children": [{"type": "t", "text": "Cyclin D1 promotes cell cycle progression through enhancing NDR1/2 kinase activity independent of cyclin-dependent kinase 4."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M113.466433"}], "href": "https://doi.org/10.1074/jbc.M113.466433"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23897809"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23897809"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Takemichi Fukasawa, Atsushi Enomoto, Kiyoshi Miyagawa "}, {"type": "b", "children": [{"type": "t", "text": "Serine-Threonine Kinase 38 regulates CDC25A stability and the DNA damage-induced G2/M checkpoint."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Signal (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellsig.2015.04.013"}], "href": "https://doi.org/10.1016/j.cellsig.2015.04.013"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25936524"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25936524"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Maomao Yan, Lingluo Chu, Bo Qin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Regulation of NDR1 activity by PLK1 ensures proper spindle orientation in mitosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/srep10449"}], "href": "https://doi.org/10.1038/srep10449"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26057687"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26057687"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Carine Joffre, Nicolas Dupont, Lily Hoa, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Pro-apoptotic STK38 Kinase Is a New Beclin1 Partner Positively Regulating Autophagy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Curr Biol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cub.2015.08.031"}], "href": "https://doi.org/10.1016/j.cub.2015.08.031"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26387716"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26387716"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Audrey Bettoun, Carine Joffre, Giulia Zago, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial clearance by the STK38 kinase supports oncogenic Ras-induced cell transformation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.9875"}], "href": "https://doi.org/10.18632/oncotarget.9875"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27283898"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27283898"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Atsushi Enomoto, Naoki Kido, Michihiko Ito, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Serine-threonine kinase 38 is regulated by glycogen synthase kinase-3 and modulates oxidative stress-induced cell death."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Free Radic Biol Med (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.freeradbiomed.2011.11.006"}], "href": "https://doi.org/10.1016/j.freeradbiomed.2011.11.006"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22142472"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22142472"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Monami Ogura, Tatsuya Kaminishi, Takayuki Shima, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Microautophagy regulated by STK38 and GABARAPs is essential to repair lysosomes and prevent aging."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO Rep (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.15252/embr.202357300"}], "href": "https://doi.org/10.15252/embr.202357300"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37987447"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37987447"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Alexandre Pj Martin, Maarten Jacquemyn, Joanna Lipecka, et al. "}, {"type": "b", "children": [{"type": "t", "text": "STK38 kinase acts as XPO1 gatekeeper regulating the nuclear export of autophagy proteins and other cargoes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO Rep (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.15252/embr.201948150"}], "href": "https://doi.org/10.15252/embr.201948150"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31544310"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31544310"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Alexandre Pj Martin, Vasily N Aushev, Gérard Zalcman, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The STK38-XPO1 axis, a new actor in physiology and cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Mol Life Sci (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00018-020-03690-w"}], "href": "https://doi.org/10.1007/s00018-020-03690-w"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33145612"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33145612"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Indranil Paul, Tanveer S Batth, Diego Iglesias-Gato, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The ubiquitin ligase Cullin5"}, {"type": "a", "children": [{"type": "t", "text": "sup"}], "href": "sup"}, {"type": "t", "text": "SOCS2"}, {"type": "a", "children": [{"type": "t", "text": "/sup"}], "href": "/sup"}, {"type": "t", "text": " regulates NDR1/STK38 stability and NF-κB transactivation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/srep42800"}], "href": "https://doi.org/10.1038/srep42800"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28216640"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28216640"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Dan-Dan Shi, Hu Shi, Dan Lu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "NDR1/STK38 potentiates NF-κB activation by its kinase activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Biochem Funct (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/cbf.2846"}], "href": "https://doi.org/10.1002/cbf.2846"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22674419"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22674419"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Zhiyong Liu, Qiang Qin, Cheng Wu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Downregulated NDR1 protein kinase inhibits innate immune response by initiating an miR146a-STAT1 feedback loop."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-018-05176-7"}], "href": "https://doi.org/10.1038/s41467-018-05176-7"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30018336"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30018336"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Cheng-Dong Ji, Yan-Xia Wang, Dong-Fang Xiang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Kir2.1 Interaction with Stk38 Promotes Invasion and Metastasis of Human Gastric Cancer by Enhancing MEKK2-MEK1/2-ERK1/2 Signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-17-3776"}], "href": "https://doi.org/10.1158/0008-5472.CAN-17-3776"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29549164"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29549164"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "B C Bisikirska, S J Adam, M J Alvarez, et al. "}, {"type": "b", "children": [{"type": "t", "text": "STK38 is a critical upstream regulator of MYC's oncogenic activity in human B-cell lymphoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2012.543"}], "href": "https://doi.org/10.1038/onc.2012.543"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23178486"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23178486"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Isabelle Pot, Shachi Patel, Lili Deng, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of a Novel Link between the Protein Kinase NDR1 and TGFβ Signaling in Epithelial Cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0067178"}], "href": "https://doi.org/10.1371/journal.pone.0067178"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23840619"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23840619"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Atsushi Enomoto, Takemichi Fukasawa, Nobuhiko Takamatsu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The HSP90 inhibitor 17-allylamino-17-demethoxygeldanamycin modulates radiosensitivity by downregulating serine/threonine kinase 38 via Sp1 inhibition."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Cancer (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ejca.2013.06.034"}], "href": "https://doi.org/10.1016/j.ejca.2013.06.034"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23886587"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23886587"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Eric Devroe, Pamela A Silver, Alan Engelman "}, {"type": "b", "children": [{"type": "t", "text": "HIV-1 incorporates and proteolytically processes human NDR1 and NDR2 serine-threonine kinases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Virology (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.virol.2004.10.023"}], "href": "https://doi.org/10.1016/j.virol.2004.10.023"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15582665"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15582665"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Yankuo Liu, Zhiyuan Shi, Zeyuan Zheng, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Prognostic and Immunological Role of "}, {"type": "a", "children": [{"type": "t", "text": "i"}], "href": "i"}, {"type": "t", "text": "STK38"}, {"type": "a", "children": [{"type": "t", "text": "/i"}], "href": "/i"}, {"type": "t", "text": " across Cancers: Friend or Foe?"}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Mol Sci (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/ijms231911590"}], "href": "https://doi.org/10.3390/ijms231911590"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36232893"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36232893"}]}, {"type": "r", "ref": 29, "children": [{"type": "t", "text": "Kun Qian, Daozhan Yu, Weiming Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "STK38 is a PPARγ-interacting protein promoting adipogenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Adipocyte (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/21623945.2021.1980257"}], "href": "https://doi.org/10.1080/21623945.2021.1980257"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34670478"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34670478"}]}, {"type": "r", "ref": 30, "children": [{"type": "t", "text": "Ling-Ling Wang, Xiao-Yun Wan, Chun-Qi Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "NDR1 increases NOTCH1 signaling activity by impairing Fbw7 mediated NICD degradation to enhance breast cancer stem cell properties."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Med (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s10020-022-00480-x"}], "href": "https://doi.org/10.1186/s10020-022-00480-x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35508987"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35508987"}]}]}]}