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Literature summary for 2.4.1.144 extracted from

  • Sato, Y.; Isaji, T.; Tajiri, M.; Yoshida-Yamamoto, S.; Yoshinaka, T.; Somehara, T.; Fukuda, T.; Wada, Y.; Gu, J.
    An N-glycosylation site on the beta-propeller domain of the integrin alpha5 subunit plays key roles in both its function and site-specific modification by beta1,4-N-acetylglucosaminyltransferase III (2009), J. Biol. Chem., 284, 11873-11881.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
amplified for cloning into pENTR-D-Topo vector, cloned gene inserted into the virus expression vector, pBABE-puro. GnT-III and GnT-V constructs transfected into Phoenix-Ampho cells Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
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 Homo sapiens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information GnT-III selectively modifies N-glycosylation site-4 on the integrin alpha5 subunit (S-3,4,5), which down-regulates its biological functions Homo sapiens ?
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 ?

Synonyms

Synonyms Comment Organism
beta1,4-N-acetylglucosaminyltransferase III
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 Homo sapiens
GnT-III
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 Homo sapiens

General Information

General Information Comment Organism
physiological function introduction of GnT-III suppresses additional processing and branching formation of N-glycans catalyzed by other endogenous glycosyltransferases, such as GnT-V and GnT-IV. Cell adhesion on fibronectin is down-regulated in GnT-III transfectants compared with mock and GnT-V transfectants. Overexpression of GnT-III significantly inhibits cell migration on fibronectin. GnT-III significantly down-regulates cell spreading on fibronectin in wild-type transfectants, whereas the deletion of site-4 abolishes the suppression of cell spread induced by GnT-III in D-4 transfectants Homo sapiens