The putative tumor suppressors EXT1 and EXT2 form a stable complex that accumulates in the Golgi apparatus and catalyzes the synthesis of heparan sulfate.
By C. McCormick, Gillian Duncan, K. T. Goutsos, F. Tufaro. 2000
468 citations recorded by the source corpus.
Subfields: Oral Surgery, Pulmonary and Respiratory Medicine, Rheumatology
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Citations in the corpus
- Mutations in EXTL3 Cause Neuro-immuno-skeletal Dysplasia Syndrome. (2017, background): “Regarding human disorders, EXT1 (MIM: 608177) and EXT2 (MIM: 608210) are associated with autosomal-dominant hereditary multiple exostoses (MIM: 133700 and 133701, respectively).(15) In addition, autosomal-recessive mutations in EXT2 lead to seizures, scoliosis, and macrocephaly syndrome (MIM: 616682”
- The exostosin family: proteins with many functions. (2014, unknown): “1) involved in HS elongation (Lind et al., 1998; McCormick et al., 2000; Senay et al., 2000).”
- The roles of enzyme localisation and complex formation in glycan assembly within the Golgi apparatus. (2004, result): “Each enzyme expressed separately was found localised in the ER, inconsistent with previous work suggesting that heparan sulfate chain extension occurs inside the Golgi [40].”
- Hereditary multiple exostoses and heparan sulfate polymerization. (2002, background): “Secondly, etiologic mutations in this region lack GlcA transferase activity, suggesting that the active site is nearby [37].”
- EXTL3 mutations cause skeletal dysplasia, immune deficiency, and developmental delay (2017, background): “EXT2 is involved in HS biosynthesis (McCormick et al., 2000; Senay et al., 2000) but has no known role in REG protein signaling.”
- Organization of Golgi Glycosyltransferases in Membranes: Complexity via Complexes (2004, background): “First, EXT1 and EXT2 have attracted special interest because most cases of hereditary multiple exostoses have been attributed to mutations in either one of these genes.”
- Determinants of Glycosaminoglycan (GAG) Structure (2015, background): “involved in HS polymerization, must associate in the ER to move forward to the Golgi apparatus [152].”
- Glycosyltransferase complexes in eukaryotes: long-known, prevalent but still unrecognized (2015, background): “[72] have shown that EXT1 and EXT2 (both of which have GlcA-and GlcNAc-transferase activities and contribute to heparan sulfate biosynthesis [73] ) form not only enzyme homomers but also heteromers both in yeast and mammalian cells.”