Subcellular localization and substrate specificity of dolichol kinase from rat liver

Keller, R. Kennedy; Rottler, Grant D.; Cafmeyer, Nancy; Adair, W. Lee

doi:10.1016/0304-4165(82)90315-4

Cited by 35 publications

(1 citation statement)

References 33 publications

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“…The inset table presents the ratio of polyprenol to dolichol (see Figure 2 B), as well as the ratios of the corresponding phospho and phosphohexose derivatives (A and B) (means ± SEM, n = 4). The percentages alongside red dashed lines indicate the relative activity of the indicated enzyme when using a polyprenol-instead of dolichol-derived substrate (DOLK, dolichol kinase 40 ; DPM1/2/3, Dolichol-phosphate mannosyltransferase 41 ; ALG3, Alpha-1,3-Mannosyltransferase 42 ; DPAGT1, UDP-N-acetylglucosamine—dolichyl-phosphate N-acetylglucosamine-phosphotransferase 43 , 44 . Erroneous transfer of an immature glycan (Man 5 GlcNAc 2 ) to nascent glycoproteins leads to linear Man-5 NLOs (see “abnormal glycosylation” box), that are subsequently trimmed to Man-4 NLOs by the enzyme EDEM3.…”

Section: Resultsmentioning

confidence: 99%

A pseudoautosomal glycosylation disorder prompts the revision of dolichol biosynthesis

Wilson,

Kentache,

Althoff

et al. 2024

Cell

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Section: Resultsmentioning

confidence: 99%

A pseudoautosomal glycosylation disorder prompts the revision of dolichol biosynthesis

Wilson,

Kentache,

Althoff

et al. 2024

Cell

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Reduced utilization of Man5GlcNAc2-P-P-lipid in a Lec9 mutant of Chinese hamster ovary cells: Analysis of the steps in oligosaccharide-lipid assembly

et al. 1997

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Recently we reported that CHB11-1-3, a Chinese hamster ovary cell mutant defective in glycosylation of asparagine-linked proteins, is defective in the synthesis of dolichol [Quellhorst et al., 343:19-26, 1997: Arch Biochem Biophys]. CHB11-1-3 was found to be in the Lec9 complementation group, which synthesizes polyprenol rather than dolichol. In this paper, levels of various polyprenyl derivatives in CHB11-1-3 are compared to levels of the corresponding dolichyl derivatives in parental cells. CHB11-1-3 was found to maintain near normal levels of Man5GlcNAc2-P-P-polyprenol and mannosylphosphorylpolyprenol, despite reduced rates of synthesis, by utilizing those intermediates at a reduced rate. The Man5GlcNAc2 oligosaccharide attached to prenol in CHB11-1-3 cells and to dolichol in parental cells is the same structure, as determined by acetolysis. Man5GlcNAc2-P-P-polyprenol and Man5GlcNAc5-P-P-dolichol both appeared to be translocated efficiently in an in vitro reaction. Glycosylation of G protein was compared in vesicular stomatitus virus (VSV)-infected parent and mutant; although a portion of G protein was compared in vesicular stomatitus virus (VSV)-infected parent and mutant; although a portion of G protein was normally glycosylated in CHB11-1-3 cells, a large portion of G was underglycosylated, resulting in the addition of either one or no oligosaccharide to G. Addition of a single oligosaccharide occurred randomly rather than preferentially at one of the two sites.

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The Importance of Being Dolichol

Krag

1998

Biochemical and Biophysical Research Communications

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Subcellular localization and substrate specificity of dolichol kinase from rat liver

Cited by 35 publications

References 33 publications

A pseudoautosomal glycosylation disorder prompts the revision of dolichol biosynthesis

A pseudoautosomal glycosylation disorder prompts the revision of dolichol biosynthesis

Reduced utilization of Man5GlcNAc2-P-P-lipid in a Lec9 mutant of Chinese hamster ovary cells: Analysis of the steps in oligosaccharide-lipid assembly

The Importance of Being Dolichol

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