Gene Symbol: Gba2
Description: glucosidase beta 2
Alias: F630034E04, non-lysosomal glucosylceramidase, NLGase, beta-glucocerebrosidase 2, beta-glucosidase 2, bile acid, glucosidase, beta (bile acid) 2, glucosylceramidase 2
Species: mouse
Products:     Gba2

Top Publications

  1. Yildiz Y, Matern H, Thompson B, Allegood J, Warren R, Ramirez D, et al. Mutation of beta-glucosidase 2 causes glycolipid storage disease and impaired male fertility. J Clin Invest. 2006;116:2985-94 pubmed
    ..2 (GBA2) is a resident enzyme of the endoplasmic reticulum thought to play a role in the metabolism of bile acid-glucose conjugates...
  2. Körschen H, Yildiz Y, Raju D, Schonauer S, Bönigk W, Jansen V, et al. The non-lysosomal ?-glucosidase GBA2 is a non-integral membrane-associated protein at the endoplasmic reticulum (ER) and Golgi. J Biol Chem. 2013;288:3381-93 pubmed publisher
    GBA1 and GBA2 are both ?-glucosidases, which cleave glucosylceramide (GlcCer) to glucose and ceramide. GlcCer is a main precursor for higher order glycosphingolipids but might also serve as intracellular messenger...
  3. Ridley C, Thur K, Shanahan J, Thillaiappan N, Shen A, Uhl K, et al. ?-Glucosidase 2 (GBA2) activity and imino sugar pharmacology. J Biol Chem. 2013;288:26052-66 pubmed publisher
    Glucosidase 2 (GBA2) is an enzyme that cleaves the membrane lipid glucosylceramide into glucose and ceramide. The GBA2 gene is mutated in genetic neurological diseases (hereditary spastic paraplegia and cerebellar ataxia)...
  4. Mistry P, Liu J, Sun L, Chuang W, Yuen T, Yang R, et al. Glucocerebrosidase 2 gene deletion rescues type 1 Gaucher disease. Proc Natl Acad Sci U S A. 2014;111:4934-9 pubmed publisher
    ..How metabolites of GL-1 or LysoGL-1 produced by extralysosomal glucocerebrosidase GBA2 contribute to the GD1 pathophysiology is not known...
  5. Marques A, Aten J, Ottenhoff R, van Roomen C, Herrera Moro D, Claessen N, et al. Reducing GBA2 Activity Ameliorates Neuropathology in Niemann-Pick Type C Mice. PLoS ONE. 2015;10:e0135889 pubmed publisher
    ..Besides lysosomal GBA, cells also contain a non-lysosomal glucosylceramidase (GBA2)...
  6. Walden C, Sandhoff R, Chuang C, Yildiz Y, Butters T, Dwek R, et al. Accumulation of glucosylceramide in murine testis, caused by inhibition of beta-glucosidase 2: implications for spermatogenesis. J Biol Chem. 2007;282:32655-64 pubmed
    ..into glucose and ceramide, is sensitive to imino sugars in vitro, and has been characterized as beta-glucosidase 2 (GBA2). Imino sugars raised the level of glucosylceramide in brain, spleen, and testis, in a dose-dependent fashion...
  7. Harzer K, Blech Hermoni Y, Goldin E, Felderhoff Mueser U, Igney C, Sidransky E, et al. Beta-glucosidase 1 (GBA1) is a second bile acid β-glucosidase in addition to β-glucosidase 2 (GBA2). Study in β-glucosidase deficient mice and humans. Biochem Biophys Res Commun. 2012;423:308-12 pubmed publisher
    ..Before the leading role of glucosylceramide was recognised for both deficient conditions, bile acid-3-O-β-glucoside (BG), another natural substrate, was viewed as the main substrate of GBA2...
  8. Gonzalez Carmona M, Sandhoff R, Tacke F, Vogt A, Weber S, Canbay A, et al. Beta-glucosidase 2 knockout mice with increased glucosylceramide show impaired liver regeneration. Liver Int. 2012;32:1354-62 pubmed publisher
    ..We previously generated beta-glucosidase 2 (GBA2) knockout mice that accumulate the glycolipid glucosylceramide in various tissues, including the liver...
  9. Marques A, Mirzaian M, Akiyama H, Wisse P, Ferraz M, Gaspar P, et al. Glucosylated cholesterol in mammalian cells and tissues: formation and degradation by multiple cellular β-glucosidases. J Lipid Res. 2016;57:451-63 pubmed publisher
    ..Cells express two GlcCer-degrading β-glucosidases, glucocerebrosidase (GBA) and GBA2, located in and outside the lysosome, respectively...

More Information


  1. Boot R, Verhoek M, Donker Koopman W, Strijland A, van Marle J, Overkleeft H, et al. Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2. J Biol Chem. 2007;282:1305-12 pubmed
    ..We here report that the non-lysosomal glucosylceramidase is identical to the earlier described bile acid beta-glucosidase, being beta-glucosidase 2 (GBA2)...
  2. Shelkovnikova T, Peters O, Deykin A, Connor Robson N, Robinson H, Ustyugov A, et al. Fused in sarcoma (FUS) protein lacking nuclear localization signal (NLS) and major RNA binding motifs triggers proteinopathy and severe motor phenotype in transgenic mice. J Biol Chem. 2013;288:25266-74 pubmed publisher
    ..Our data indicate that neuronal FUS aggregation is sufficient to cause ALS-like phenotype in transgenic mice. ..
  3. Raju D, Schonauer S, Hamzeh H, FLYNN K, Bradke F, Vom Dorp K, et al. Accumulation of glucosylceramide in the absence of the beta-glucosidase GBA2 alters cytoskeletal dynamics. PLoS Genet. 2015;11:e1005063 pubmed publisher
    ..Here, we reveal that glucosylceramide accumulation in GBA2 knockout-mice alters cytoskeletal dynamics due to a more ordered lipid organization in the plasma membrane...
  4. Schonauer S, Körschen H, Penno A, Rennhack A, Breiden B, Sandhoff K, et al. Identification of a feedback loop involving β-glucosidase 2 and its product sphingosine sheds light on the molecular mechanisms in Gaucher disease. J Biol Chem. 2017;292:6177-6189 pubmed publisher
    The lysosomal acid β-glucosidase GBA1 and the non-lysosomal β-glucosidase GBA2 degrade glucosylceramide (GlcCer) to glucose and ceramide in different cellular compartments...
  5. Sun Y, Liou B, Quinn B, Ran H, Xu Y, Grabowski G. In vivo and ex vivo evaluation of L-type calcium channel blockers on acid beta-glucosidase in Gaucher disease mouse models. PLoS ONE. 2009;4:e7320 pubmed publisher
    ..These results show that LTCC blockers had the ex vivo effects of increasing GCase activity and protein in the mouse fibroblasts, but these effects did not translate into similar changes in vivo even at very high drug doses. ..
  6. Blanz J, Groth J, Zachos C, Wehling C, Saftig P, Schwake M. Disease-causing mutations within the lysosomal integral membrane protein type 2 (LIMP-2) reveal the nature of binding to its ligand beta-glucocerebrosidase. Hum Mol Genet. 2010;19:563-72 pubmed publisher
  7. von Gerichten J, Schlosser K, Lamprecht D, Morace I, Eckhardt M, Wachten D, et al. Diastereomer-specific quantification of bioactive hexosylceramides from bacteria and mammals. J Lipid Res. 2017;58:1247-1258 pubmed publisher
    ..Finally, this method is shown to separate corresponding hexosylsphingosine standards, promoting its applicability in further investigations. ..