Glycosylation of nuclear pore protein p62. Reticulocyte lysate catalyzes O-linked N-acetylglucosamine addition in vitro

Starr, C M; Hanover, J A

doi:10.1016/s0021-9258(19)39229-4

Cited by 87Glycosylation and Glycoproteins ResearchNuclear Structure and FunctionCarbohydrate Chemistry and Synthesis

Glycosylation of nuclear pore protein p62. Reticulocyte lysate catalyzes O-linked N-acetylglucosamine addition in vitro

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Starr, C M, Hanover, J A·1990·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(19)39229-4

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Abstract

The addition of O-linked N-acetylglucosamine (GlcNAc) to the major nuclear pore complex glycoprotein p62 was examined. Expression of the rat p62 cDNA in transfected monkey cells was detected using a rat p62-specific antipeptide antiserum and two previously described nuclear pore-specific monoclonal antibodies which require O-linked GlcNAc for binding. Although the p62 cDNA was predicted to encode a 54-kDa polypeptide, the product expressed in monkey cells migrated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis as two species of 62 and 59-kDa. Cell-free translation of the p62 in vitro transcript yielded a 59-kDa polypeptide using wheat germ extract and a 62-kDa product using a commercially available rabbit reticulocyte lysate. Several lines of evidence indicated that the 62-kDa rabbit reticulocyte lysate translation product was modified by O-linked N-acetylglucosamine; the protein bound specifically to a wheat germ agglutinin affinity column and was converted to 59 kDa when treated with jack bean beta-acetylglucosaminidase. The 59-kDa unglycosylated wheat germ translation product was converted to the 62-kDa glycosylated form upon incubation with reticulocyte lysate demonstrating that O-linked GlcNAc can be added to p62 post-translationally.

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Autoimmune Antibodies to hnRNPG Protein in Dogs with Systemic Lupus Erythematosus: Epitope Mapping of the Antigen
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Self-citation
Mitochondrial and nucleocytoplasmic targeting of O-linked GlcNAc transferase
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Cell-Free Synthetic Biology
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Analysis of nuclear pore protein p62 glycosylation
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Primary Sequence and Heterologous Expression of Nuclear Pore Glycoprotein p62
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An Evaluation of Sialation of the Nucleoporin p62
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Self-citation

Authors: Starr, C. M., & Hanover, J. A.
Affiliations: National Institutes of Health (US)
ORCID: Hanover, J A
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1990-04
Volume: 265
Issue: 12
Pages: 6868-6873
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(19)39229-4
OpenAlex: W1556106321
Cited by: 87
References: 19
Citations by year: 2026: 1 · 2025: 1 · 2022: 3 · 2021: 2 · 2019: 3 · 2018: 3 · 2017: 2 · 2016: 3 · 2015: 4
FWCI: 1.43
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 11167 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
Keywords: p62, nuclear pore complex, O-glycosylation, N-acetylglucosamine, reticulocyte lysate, post-translational modification, glycoproteins, wheat germ agglutinin binding, cDNA expression, glycosylation sites
MeSH terms: Acetylglucosamine, Amino Acid Sequence, Animals, Antibodies, Monoclonal, Cell Line, Chromatography, Affinity, DNA, Fluorescent Antibody Technique, Glucosamine, Glycosylation, Membrane Glycoproteins, Membrane Proteins, Molecular Sequence Data, Molecular Weight, Protein Processing, Post-Translational, Reticulocytes, Transfection, Protein Biosynthesis, Nuclear Pore Complex Proteins, Rats

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Glycosylation of nuclear pore protein p62. Reticulocyte lysate catalyzes O-linked N-acetylglucosamine addition in vitro

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