1997
DOI: 10.1073/pnas.94.7.2897
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Abstract: By expression cloning using COS-1 cells stably transfected with GD3-synthase (COS-1͞GD3؉ ) as a recipient cell line, we have isolated a cDNA, termed AT-1, encoding a novel protein required for the formation of Oacetylated (Ac) gangliosides. The cDNA encodes a protein with multitransmembrane spanning domains with a leucine zipper motif. It consists of 549 amino acids and has a molecular mass of 60.9 kDa. Although both O-Ac-GD3 and O-Ac-GT3 were barely detectable in recipient cells or cells transfected with the … Show more

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Cited by 84 publications
(59 citation statements)
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“…In 1997, Kanamori et al reported the identification of a new protein (AT-1) that appeared to affect the acetylation of complex gangliosides in the secretory pathway (Kanamori et al, 1997). The authors were interested in the Golgi-resident acetyltransferase responsible for the O-acetylation of complex gangliosides but, surprisingly, the new protein displayed a possible ER localization in addition to features that were consistent with membrane transporters rather than acetyltransferases.…”
Section: Introductionmentioning
confidence: 99%
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“…In 1997, Kanamori et al reported the identification of a new protein (AT-1) that appeared to affect the acetylation of complex gangliosides in the secretory pathway (Kanamori et al, 1997). The authors were interested in the Golgi-resident acetyltransferase responsible for the O-acetylation of complex gangliosides but, surprisingly, the new protein displayed a possible ER localization in addition to features that were consistent with membrane transporters rather than acetyltransferases.…”
Section: Introductionmentioning
confidence: 99%
“…As a result, the authors proposed a possible role as ER membrane acetyl-CoA transporter and named the new protein acetylCoenzyme A transporter 1 (AT-1) (Hirabayashi et al, 2004;Kanamori et al, 1997). However, no functional proof was provided regarding the biochemical activity or properties of this protein.…”
Section: Introductionmentioning
confidence: 99%
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“…Others have also attempted to isolate the 9-O-acetyltransferase without success. In one study, a putative acetyl-CoA transporter that induced 9-O-acetylation of GD3 was isolated through expression cloning (36). However, this protein has an ortholog in yeasts (which do not express sialic acids) and is predominantly expressed in the endoplasmic reticulum.…”
Section: -O-acetylation Of Sialic Acid On N-glycans Is Notmentioning
confidence: 99%
“…The 9-O-acetyltransferase activity in most systems is very sensitive to solubilization, and thus, direct purification has proven difficult (27,28,34). Heterologous cell-cDNA library pairs were applied by several investigators to the attempted expression cloning of a 9-O-acetyltransferase cDNA in COS cells (35)(36)(37). However, whereas several candidate genes were isolated, neither a 9-O-acetyltransferase nor a biologically significant inducer for 9-O-acetylation was eventually defined.…”
mentioning
confidence: 99%