{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPKCζ plays a central role in coordinating immune and inflammatory responses. In neutrophils, for example, it contributes to the phosphorylation of cytosolic oxidase components that boost superoxide production, while in endothelial cells it helps relay thrombin‐ and cytokine‐induced signals that activate NF‑κB and stimulate VCAM‑1 expression. Moreover, PKCζ is required for chemokine (SDF‑1)–mediated cell polarization, migration, and adhesion of hematopoietic progenitors, and its association with adaptor proteins (such as Ajuba) further amplifies NF‑κB‐dependent inflammatory signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the vascular and endothelial compartment, PKCζ regulates key aspects of blood vessel morphogenesis and homeostasis. It participates in endothelial lumen and tube formation by interfacing with polarity complexes, and it phosphorylates upstream enzymes like LKB1 to activate AMPK—linking metabolic cues to vascular function. Under disturbed flow conditions, PKCζ becomes aberrantly activated, triggering modifications of p53 and destabilization of endothelial nitric‐oxide synthase that contribute to cell apoptosis and atherogenesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nWithin the context of insulin signaling and metabolic regulation, PKCζ modulates the activity of key mediators of glucose homeostasis. It phosphorylates insulin receptor substrate‑1 on specific serine residues to regulate its interaction with the insulin receptor, thereby helping to control insulin‐stimulated glucose transport in skeletal muscle and adipose tissue."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPKCζ also orchestrates cell polarity and cytoskeletal dynamics, processes fundamental to neuronal function and host–pathogen interactions. It interacts with components of the polarity complex (via factors such as ECT2 and Par proteins) and phosphorylates substrates like KIBRA and myosin II‑B to regulate filament assembly, synaptic targeting (including the palmitoylation and trafficking of PSD‑95), and directional cell migration. In addition, PKCζ supports the invasion of host cells by pathogens—in one study facilitating Plasmodium sporozoite entry into hepatocytes."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the regulation of apoptosis and cell survival, PKCζ acts as a critical checkpoint by phosphorylating pro‐apoptotic proteins and caspases. Its modification of caspase‑9 and Bax contributes to the suppression of apoptotic cascades under stress conditions. Furthermore, by enabling phosphorylation events that modulate neurofibromin signaling, PKCζ influences cAMP levels and cell survival pathways."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nStudies in cancer models illustrate that PKCζ can function as a tumor suppressor and as a regulator of malignant cell behavior. In certain tumor cells, loss or inhibition of PKCζ promotes metabolic reprogramming—for example, through enhanced glutamine utilization and activation of serine biosynthetic pathways—as well as increased invasive potential. Such findings underscore its dual role in restraining tumor progression and in modulating cell adhesion and matrix remodeling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "24", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, PKCζ participates in additional signaling contexts that affect hormonal gene regulation and immune development. In relaxin signaling, for instance, PKCζ is activated in a phosphoinositide‐3 kinase–dependent manner to stimulate a biphasic cAMP response. It also mediates the derepression of luteinizing hormone receptor gene expression via Sp1 phosphorylation and contributes to the maturation of neonatal T cells, processes influenced by environmental factors."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Alexandre Fontayne, Pham My-Chan Dang, Marie-Anne Gougerot-Pocidalo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Phosphorylation of p47phox sites by PKC alpha, beta II, delta, and zeta: effect on binding to p22phox and on NADPH oxidase activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/bi011953s"}], "href": "https://doi.org/10.1021/bi011953s"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12056906"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12056906"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Takashi Minami, Md Ruhul Abid, Jie Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Thrombin stimulation of vascular adhesion molecule-1 in endothelial cells is mediated by protein kinase C (PKC)-delta-NF-kappa B and PKC-zeta-GATA signaling pathways."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M208974200"}], "href": "https://doi.org/10.1074/jbc.M208974200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12493764"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12493764"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Suzana D Savkovic, Athanasia Koutsouris, Gail Hecht "}, {"type": "b", "children": [{"type": "t", "text": "PKC zeta participates in activation of inflammatory response induced by enteropathogenic E. coli."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Cell Physiol (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpcell.00444.2002"}], "href": "https://doi.org/10.1152/ajpcell.00444.2002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12900386"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12900386"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Nicole Teusch, Eleuterio Lombardo, Jane Eddleston, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The low molecular weight GTPase RhoA and atypical protein kinase Czeta are required for TLR2-mediated gene transcription."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.173.1.507"}], "href": "https://doi.org/10.4049/jimmunol.173.1.507"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15210811"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15210811"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Isabelle Petit, Polina Goichberg, Asaf Spiegel, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Atypical PKC-zeta regulates SDF-1-mediated migration and development of human CD34+ progenitor cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Invest (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1172/JCI21773"}], "href": "https://doi.org/10.1172/JCI21773"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15630457"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15630457"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Edward R LaVallie, Priya S Chockalingam, Lisa A Collins-Racie, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein kinase Czeta is up-regulated in osteoarthritic cartilage and is required for activation of NF-kappaB by tumor necrosis factor and interleukin-1 in articular chondrocytes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M601905200"}], "href": "https://doi.org/10.1074/jbc.M601905200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16798739"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16798739"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Alexandra C Newton "}, {"type": "b", "children": [{"type": "t", "text": "Protein kinase C as a tumor suppressor."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Semin Cancer Biol (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.semcancer.2017.04.017"}], "href": "https://doi.org/10.1016/j.semcancer.2017.04.017"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28476658"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28476658"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Laura A Dada, Navdeep S Chandel, Karen M Ridge, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hypoxia-induced endocytosis of Na,K-ATPase in alveolar epithelial cells is mediated by mitochondrial reactive oxygen species and PKC-zeta."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Invest (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1172/JCI16826"}], "href": "https://doi.org/10.1172/JCI16826"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12671055"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12671055"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Zhonglin Xie, Yunzhou Dong, Miao Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Activation of protein kinase C zeta by peroxynitrite regulates LKB1-dependent AMP-activated protein kinase in cultured endothelial cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M511178200"}], "href": "https://doi.org/10.1074/jbc.M511178200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16407220"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16407220"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Wonshill Koh, Rachel D Mahan, George E Davis "}, {"type": "b", "children": [{"type": "t", "text": "Cdc42- and Rac1-mediated endothelial lumen formation requires Pak2, Pak4 and Par3, and PKC-dependent signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.020693"}], "href": "https://doi.org/10.1242/jcs.020693"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18319301"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18319301"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Patrizia Nigro, Jun-ichi Abe, Chang-Hoon Woo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PKCzeta decreases eNOS protein stability via inhibitory phosphorylation of ERK5."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2010-02-269134"}], "href": "https://doi.org/10.1182/blood-2010-02-269134"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20538799"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20538799"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Kyung-Sun Heo, Hakjoo Lee, Patrizia Nigro, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PKCζ mediates disturbed flow-induced endothelial apoptosis via p53 SUMOylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.201010051"}], "href": "https://doi.org/10.1083/jcb.201010051"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21624955"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21624955"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Mary Beeson, Mini P Sajan, Michelle Dizon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Activation of protein kinase C-zeta by insulin and phosphatidylinositol-3,4,5-(PO4)3 is defective in muscle in type 2 diabetes and impaired glucose tolerance: amelioration by rosiglitazone and exercise."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Diabetes (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2337/diabetes.52.8.1926"}], "href": "https://doi.org/10.2337/diabetes.52.8.1926"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12882907"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12882907"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Klaus Moeschel, Alexander Beck, Cora Weigert, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein kinase C-zeta-induced phosphorylation of Ser318 in insulin receptor substrate-1 (IRS-1) attenuates the interaction with the insulin receptor and the tyrosine phosphorylation of IRS-1."}]}, {"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.M402477200"}], "href": "https://doi.org/10.1074/jbc.M402477200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15069075"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15069075"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Tamara Frankenberg, Tamir Miloh, Frank Y Chen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The membrane protein ATPase class I type 8B member 1 signals through protein kinase C zeta to activate the farnesoid X receptor."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hepatology (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/hep.22431"}], "href": "https://doi.org/10.1002/hep.22431"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18668687"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18668687"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Katrin Büther, Christian Plaas, Angelika Barnekow, et al. "}, {"type": "b", "children": [{"type": "t", "text": "KIBRA is a novel substrate for protein kinase Czeta."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2004.03.107"}], "href": "https://doi.org/10.1016/j.bbrc.2004.03.107"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15081397"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15081397"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Xiu-Fen Liu, Hiroshi Ishida, Razi Raziuddin, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Nucleotide exchange factor ECT2 interacts with the polarity protein complex Par6/Par3/protein kinase Czeta (PKCzeta) and regulates PKCzeta activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.24.15.6665-6675.2004"}], "href": "https://doi.org/10.1128/MCB.24.15.6665-6675.2004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15254234"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15254234"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Liron Even-Faitelson, Shoshana Ravid "}, {"type": "b", "children": [{"type": "t", "text": "PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.e05-11-1001"}], "href": "https://doi.org/10.1091/mbc.e05-11-1001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16611744"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16611744"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Miguel Prudêncio, Cristina D Rodrigues, Michael Hannus, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Kinome-wide RNAi screen implicates at least 5 host hepatocyte kinases in Plasmodium sporozoite infection."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS Pathog (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.ppat.1000201"}], "href": "https://doi.org/10.1371/journal.ppat.1000201"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18989463"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18989463"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Akira Yoshii, Yasunobu Murata, Jihye Kim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TrkB and protein kinase Mζ regulate synaptic localization of PSD-95 in developing cortex."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurosci (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1523/JNEUROSCI.2190-11.2011"}], "href": "https://doi.org/10.1523/JNEUROSCI.2190-11.2011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21849550"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21849550"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Suzanne C Brady, Lindsey A Allan, Paul R Clarke "}, {"type": "b", "children": [{"type": "t", "text": "Regulation of caspase 9 through phosphorylation by protein kinase C zeta in response to hyperosmotic stress."}]}, {"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.25.23.10543-10555.2005"}], "href": "https://doi.org/10.1128/MCB.25.23.10543-10555.2005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16287866"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16287866"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Meiguo Xin, Fengqin Gao, W Stratford May, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein kinase Czeta abrogates the proapoptotic function of Bax through phosphorylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M701613200"}], "href": "https://doi.org/10.1074/jbc.M701613200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17525161"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17525161"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Corina Anastasaki, David H Gutmann "}, {"type": "b", "children": [{"type": "t", "text": "Neuronal NF1/RAS regulation of cyclic AMP requires atypical PKC activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddu389"}], "href": "https://doi.org/10.1093/hmg/ddu389"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25070947"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25070947"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Michael R Paillasse, Philippe de Medina, Guillaume Amouroux, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Signaling through cholesterol esterification: a new pathway for the cholecystokinin 2 receptor involved in cell growth and invasion."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Lipid Res (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1194/jlr.M800668-JLR200"}], "href": "https://doi.org/10.1194/jlr.M800668-JLR200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19502590"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19502590"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Li Ma, Yongzhen Tao, Angeles Duran, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Control of nutrient stress-induced metabolic reprogramming by PKCζ in tumorigenesis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cell.2012.12.028"}], "href": "https://doi.org/10.1016/j.cell.2012.12.028"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23374352"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23374352"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Somnath Mazumder, Rudranil De, Subhashis Debsharma, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Indomethacin impairs mitochondrial dynamics by activating the PKCζ-p38-DRP1 pathway and inducing apoptosis in gastric cancer and normal mucosal cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.RA118.004415"}], "href": "https://doi.org/10.1074/jbc.RA118.004415"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30940726"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30940726"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Bao T Nguyen, Carmen W Dessauer "}, {"type": "b", "children": [{"type": "t", "text": "Relaxin stimulates protein kinase C zeta translocation: requirement for cyclic adenosine 3',5'-monophosphate production."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Endocrinol (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1210/me.2004-0279"}], "href": "https://doi.org/10.1210/me.2004-0279"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15604116"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15604116"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Ying Zhang, Mingjuan Liao, Maria L Dufau "}, {"type": "b", "children": [{"type": "t", "text": "Phosphatidylinositol 3-kinase/protein kinase Czeta-induced phosphorylation of Sp1 and p107 repressor release have a critical role in histone deacetylase inhibitor-mediated derepression [corrected] of transcription of the luteinizing hormone receptor gene."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biol (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/MCB.00560-06"}], "href": "https://doi.org/10.1128/MCB.00560-06"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16943418"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16943418"}]}, {"type": "r", "ref": 29, "children": [{"type": "t", "text": "Hani Harb, James Irvine, Manori Amarasekera, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The role of PKCζ in cord blood T-cell maturation towards Th1 cytokine profile and its epigenetic regulation by fish oil."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biosci Rep (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BSR20160485"}], "href": "https://doi.org/10.1042/BSR20160485"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28159873"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28159873"}]}]}]}