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    SGMS2 sphingomyelin synthase 2 [ Homo sapiens (human) ]

    Gene ID: 166929, updated on 27-Aug-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Identification of SGMS2 as a molecule involved in natural killer cell recruitment and its in-deep analysis in the liver cancer microenvironment: Evidence from large populations cohort.

    Identification of SGMS2 as a molecule involved in natural killer cell recruitment and its in-deep analysis in the liver cancer microenvironment: Evidence from large populations cohort.
    Tang W, Meng F, Li M, Li Y, Xiong W, Zhang D, Yang B.

    02/7/2024
    Sphingomyelin synthase 2 promotes the stemness of breast cancer cells via modulating NF-kappaB signaling pathway.

    Sphingomyelin synthase 2 promotes the stemness of breast cancer cells via modulating NF-κB signaling pathway.
    Feng H, Dong Y, Chen K, You Z, Weng J, Liang P, Shi F., Free PMC Article

    02/1/2024
    SGMS2 in primary osteoporosis with facial nerve palsy.

    SGMS2 in primary osteoporosis with facial nerve palsy.
    Pihlström S, Richardt S, Määttä K, Pekkinen M, Olkkonen VM, Mäkitie O, Mäkitie RE., Free PMC Article

    11/16/2023
    Clinical and Genetic Characteristics of Calvarial Doughnut Lesions with Bone Fragility in Three Families with a Reccurent SGMS2 Gene Variant.

    Clinical and Genetic Characteristics of Calvarial Doughnut Lesions with Bone Fragility in Three Families with a Reccurent SGMS2 Gene Variant.
    Merkuryeva E, Markova T, Tyurin A, Valeeva D, Kenis V, Sumina M, Sorokin I, Shchagina O, Skoblov M, Nefedova M, Khusainova R, Zakharova E, Dadali E, Kutsev S., Free PMC Article

    10/30/2023
    LARP6 suppresses colorectal cancer progression through ZNF267/SGMS2-mediated imbalance of sphingomyelin synthesis.

    LARP6 suppresses colorectal cancer progression through ZNF267/SGMS2-mediated imbalance of sphingomyelin synthesis.
    Long X, Liu X, Deng T, Chen J, Lan J, Zhang S, Zhou M, Guo D, Zhou J., Free PMC Article

    02/4/2023
    LncRNA THAP9-AS1 accelerates cell growth of esophageal squamous cell carcinoma through sponging miR-335-5p to regulate SGMS2.

    LncRNA THAP9-AS1 accelerates cell growth of esophageal squamous cell carcinoma through sponging miR-335-5p to regulate SGMS2.
    Pan Q, Li B, Zhang J, Du X, Gu D.

    01/22/2022
    Genome-wide association study of serum prostate-specific antigen levels based on 1000 Genomes imputed data in Japanese: the Japan Multi-Institutional Collaborative Cohort Study.

    Genome-wide association study of serum prostate-specific antigen levels based on 1000 Genomes imputed data in Japanese: the Japan Multi-Institutional Collaborative Cohort Study.
    Hishida A, Nakatochi M, Tamura T, Nagayoshi M, Okada R, Kubo Y, Tsukamoto M, Kadomatsu Y, Suzuki S, Nishiyama T, Kuriyama N, Watanabe I, Takezaki T, Nishimoto D, Kuriki K, Arisawa K, Katsuura-Kamano S, Mikami H, Kusakabe M, Oze I, Koyanagi YN, Nakamura Y, Kadota A, Shimanoe C, Tanaka K, Ikezaki H, Murata M, Kubo M, Momozawa Y, Takeuchi K, Wakai K, for the Japan Multi-Institutional Collaborative Cohort (J-MICC) Study Group., Free PMC Article

    11/6/2021
    Sphingomyelin synthase 2 facilitates M2-like macrophage polarization and tumor progression in a mouse model of triple-negative breast cancer.

    Sphingomyelin synthase 2 facilitates M2-like macrophage polarization and tumor progression in a mouse model of triple-negative breast cancer.
    Deng Y, Hu JC, He SH, Lou B, Ding TB, Yang JT, Mo MG, Ye DY, Zhou L, Jiang XC, Yu K, Dong JB., Free PMC Article

    09/4/2021
    Chlamydia trachomatis-infected human cells convert ceramide to sphingomyelin without sphingomyelin synthases 1 and 2.

    Chlamydia trachomatis-infected human cells convert ceramide to sphingomyelin without sphingomyelin synthases 1 and 2.
    Tachida Y, Kumagai K, Sakai S, Ando S, Yamaji T, Hanada K.

    10/10/2020
    SGMS2-dependent signaling was investigated in human monocyte-derived macrophages of nonsmokers and human bronchial epithelial (HBE) cells isolated from healthy nonsmokers and subjects with COPD. Reduced SGMS2 expression was seen in HBE cells isolated from subjects with COPD. SGMS2 overexpression reduced the production of several matrix metalloproteinases in HBE cells and monocyte-derived macrophages.

    Airway Resistance Caused by Sphingomyelin Synthase 2 Insufficiency in Response to Cigarette Smoke.
    Gupta G, Baumlin N, Poon J, Ahmed B, Chiang YP, Railwah C, Kim MD, Rivas M, Goldenberg H, Elgamal Z, Salathe M, Panwala AA, Dabo A, Huan C, Foronjy R, Jiang XC, Wadgaonkar R, Geraghty P., Free PMC Article

    08/1/2020
    Study in 6 families with rare skeletal phenotypes and osteoporosis identified a heterozygous variant in SGMS2, a gene prominently expressed in cortical bone and encoding the plasma membrane-resident sphingomyelin synthase SMS2. Four unrelated families shared the same nonsense variant, c.148C>T (p.Arg50*), whereas the other families had a missense variant, c.185T>G (p.Ile62Ser) or c.191T>G (p.Met64Arg).

    Osteoporosis and skeletal dysplasia caused by pathogenic variants in SGMS2.
    Pekkinen M, Terhal PA, Botto LD, Henning P, Mäkitie RE, Roschger P, Jain A, Kol M, Kjellberg MA, Paschalis EP, van Gassen K, Murray M, Bayrak-Toydemir P, Magnusson MK, Jans J, Kausar M, Carey JC, Somerharju P, Lerner UH, Olkkonen VM, Klaushofer K, Holthuis JC, Mäkitie O., Free PMC Article

    07/4/2020
    SGMS2 increased the expression of TGF-beta1 by upregulating ceramide, which subsequently activated the TGF-beta/Smad signalling pathway and promoted epithelial-to-mesenchymal transition in breast cancer cells, thus increasing the migration and invasiveness of breast cancer cells.

    Sphingomyelin synthase 2 promotes an aggressive breast cancer phenotype by disrupting the homoeostasis of ceramide and sphingomyelin.
    Zheng K, Chen Z, Feng H, Chen Y, Zhang C, Yu J, Luo Y, Zhao L, Jiang X, Shi F., Free PMC Article

    04/11/2020
    our results demonstrate that SMS2 can activate the Wnt/beta-catenin pathway and promote intracellular cholesterol accumulation, both of which can contribute to the induction of ER stress and finally lead to ED.

    Sphingomyelin Synthase 2 Promotes Endothelial Dysfunction by Inducing Endoplasmic Reticulum Stress.
    Hua L, Wu N, Zhao R, He X, Liu Q, Li X, He Z, Yu L, Yan N., Free PMC Article

    12/7/2019
    SMS regulates the expression and function of drug transporters P-gp and MRP2.

    SMS regulates the expression and function of P-gp and MRP2 in Caco-2 cells.
    Jin G, Li Y, Zhu Y, Du L, Yan J, Yang Q.

    09/30/2017
    findings suggest that the C-terminal tails of SMSs are involved in homodimer formation, which is required for efficient transport from the ER.

    Carboxyl-terminal Tail-mediated Homodimerizations of Sphingomyelin Synthases Are Responsible for Efficient Export from the Endoplasmic Reticulum.
    Hayashi Y, Nemoto-Sasaki Y, Matsumoto N, Tanikawa T, Oka S, Tanaka Y, Arai S, Wada I, Sugiura T, Yamashita A., Free PMC Article

    06/3/2017
    PPARdelta activation may be a potential risk of atherosclerosis through enhancing activity of SMS2

    Pharmacological Activation of Peroxisome Proliferator-Activated Receptor {Delta} Increases Sphingomyelin Synthase Activity in THP-1 Macrophage-Derived Foam Cell.
    Mou D, Yang H, Qu C, Chen J, Zhang C.

    03/25/2017
    F-actin polymerization in the region of HIV-1 membrane fusion was more prominent in Sms2-expressing cells than Sms-deficient cells.

    Sphingomyelin synthase 2, but not sphingomyelin synthase 1, is involved in HIV-1 envelope-mediated membrane fusion.
    Hayashi Y, Nemoto-Sasaki Y, Tanikawa T, Oka S, Tsuchiya K, Zama K, Mitsutake S, Sugiura T, Yamashita A., Free PMC Article

    01/3/2015
    SMS1 and SMS2 are capable of regulating TGN-mediated protein trafficking and secretion

    Sphingomyelin synthases regulate protein trafficking and secretion.
    Subathra M, Qureshi A, Luberto C., Free PMC Article

    04/14/2012
    Data indicate that the increased sphingomyelin mass was due to a rapid and highly specific activation of sphingomyelin synthases SMS1 and SMS2.

    Sphingomyelin and sphingomyelin synthase (SMS) in the malignant transformation of glioma cells and in 2-hydroxyoleic acid therapy.
    Barceló-Coblijn G, Martin ML, de Almeida RF, Noguera-Salvà MA, Marcilla-Etxenike A, Guardiola-Serrano F, Lüth A, Kleuser B, Halver JE, Escribá PV., Free PMC Article

    04/14/2012
    direct morphological evidence for the pro-atherogenic capabilities of sphingomyelin synthase 2

    Adenovirus-mediated sphingomyelin synthase 2 increases atherosclerotic lesions in ApoE KO mice.
    Wang X, Dong J, Zhao Y, Li Y, Wu M., Free PMC Article

    06/25/2011
    Observational study of gene-disease association. (HuGE Navigator)

    A systematic gene-based screen of chr4q22-q32 identifies association of a novel susceptibility gene, DKK2, with the quantitative trait of alcohol dependence symptom counts.
    Kalsi G, Kuo PH, Aliev F, Alexander J, McMichael O, Patterson DG, Walsh D, Zhao Z, Schuckit M, Nurnberger J Jr, Edenberg H, Kramer J, Hesselbrock V, Tischfield JA, Vladimirov V, Prescott CA, Dick DM, Kendler KS, Riley BP., Free PMC Article

    06/30/2010
    Data show that SMS2 acting as a bifunctional enzyme with both SM and CPE synthase activity.

    Sphingomyelin synthase SMS2 displays dual activity as ceramide phosphoethanolamine synthase.
    Ternes P, Brouwers JF, van den Dikkenberg J, Holthuis JC., Free PMC Article

    03/22/2010
    Sphingomyelin synthase 2 is one of the determinants for plasma and liver sphingomyelin levels in mice.

    Sphingomyelin synthase 2 is one of the determinants for plasma and liver sphingomyelin levels in mice.
    Liu J, Zhang H, Li Z, Hailemariam TK, Chakraborty M, Jiang K, Qiu D, Bui HH, Peake DA, Kuo MS, Wadgaonkar R, Cao G, Jiang XC., Free PMC Article

    01/21/2010
    These results suggested that posttranslational palmitoylation is important for determination of the subcellular localization of SMS2.

    Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes.
    Tani M, Kuge O.

    01/21/2010
    Both SMS1 and SMS2 contain two histidines and one aspartic acid which are conserved within the lipid phosphate phosphatase superfamily. Site-directed mutagenesis of these amino acids abolished SMS activity without altering cellular distribution.

    The domain responsible for sphingomyelin synthase (SMS) activity.
    Yeang C, Varshney S, Wang R, Zhang Y, Ye D, Jiang XC., Free PMC Article

    01/21/2010
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