DOI: 10.1073/pnas.0402889101. Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: A proteomic analysis

Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: A proteomic analysis

10.1073/pnas.0402889101

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

SUMO, a small ubiquitin-related modifier, is known to covalently attach to a number of nuclear regulatory proteins such as p53, IκB, promyelocytic leukemia protein and c-Jun. The sumoylation reaction is catalyzed by the SUMO protease, which exposes the C-terminal active glycine residue of the nascent SUMO, the heterodimeric SUMO activating enzyme, the SUMO conjugating enzyme, Ubc9, and SUMO protein ligases, in a manner similar to ubiquitinylation. Identification of SUMO-regulated proteins is hampered by the fact that many sumoylated proteins are present at a level below normal detection limit. This limitation was overcome by either in vivo overexpression of Myc-SUMO or in vitro sumoylation with excess biotin–SUMO and Ubc9. Sumoylated proteins so obtained were affinity purified or isolated by immunoprecipitation. The isolated sumoylated proteins were identified by sequence analysis using mass spectrometric methods. Results reveal that several heterogeneous nuclear ribonucleoproteins (hnRNPs), zinc finger proteins, and nuclear pore complex proteins were sumoylated. The sumoylation of hnRNP A1, hnRNP F, and hnRNP K were confirmed in vivo by coimmunoprecipitation. In view of the facts that hnRNPs have been implicated in RNA splicing, transport, stability, and translation, our findings suggest that sumoylation could play an important role in regulating mRNA metabolism.

Bibliography

Li, T., Evdokimov, E., Shen, R.-F., Chao, C.-C., Tekle, E., Wang, T., Stadtman, E. R., Yang, D. C. H., & Chock, P. B. (2004). Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: A proteomic analysis. Proceedings of the National Academy of Sciences, 101(23), 8551â8556.

Authors 9

Tianwei Li (first)
Evgenij Evdokimov (additional)
Rong-Fong Shen (additional)
Chien-Chung Chao (additional)
Ephrem Tekle (additional)
Tao Wang (additional)
Earl R. Stadtman (additional)
David C. H. Yang (additional)
P. Boon Chock (additional)

References 33 Referenced 151

10.1016/B978-0-12-152813-3.50007-0
Chock, P. B. & Stadtman, E. R. (1995) in Principles of Medical Biology, eds. Bittard, E. E. & Bittar, N. (JAI Press, Greenwich, CT), Vol. 5, pp. 199–218. / Principles of Medical Biology (1995)
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Dates

Type	When
Created	21 years, 3 months ago (May 25, 2004, 8:43 p.m.)
Deposited	3 years, 4 months ago (April 12, 2022, 9:49 a.m.)
Indexed	3 weeks ago (Aug. 7, 2025, 4:32 p.m.)
Issued	21 years, 3 months ago (May 25, 2004)
Published	21 years, 3 months ago (May 25, 2004)
Published Online	21 years, 3 months ago (May 25, 2004)
Published Print	21 years, 2 months ago (June 8, 2004)

Funders 0

None

BibTeX

@article{Li_2004, title={Sumoylation of heterogeneous nuclear ribonucleoproteins, zinc finger proteins, and nuclear pore complex proteins: A proteomic analysis}, volume={101}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0402889101}, DOI={10.1073/pnas.0402889101}, number={23}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Li, Tianwei and Evdokimov, Evgenij and Shen, Rong-Fong and Chao, Chien-Chung and Tekle, Ephrem and Wang, Tao and Stadtman, Earl R. and Yang, David C. H. and Chock, P. Boon}, year={2004}, month=may, pages={8551–8556} }

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  "abstract": "<jats:p>\n            SUMO, a small ubiquitin-related modifier, is known to covalently attach to a number of nuclear regulatory proteins such as p53, I\u03baB, promyelocytic leukemia protein and c-Jun. The sumoylation reaction is catalyzed by the SUMO protease, which exposes the C-terminal active glycine residue of the nascent SUMO, the heterodimeric SUMO activating enzyme, the SUMO conjugating enzyme, Ubc9, and SUMO protein ligases, in a manner similar to ubiquitinylation. Identification of SUMO-regulated proteins is hampered by the fact that many sumoylated proteins are present at a level below normal detection limit. This limitation was overcome by either\n            <jats:italic>in vivo</jats:italic>\n            overexpression of Myc-SUMO or\n            <jats:italic>in vitro</jats:italic>\n            sumoylation with excess biotin\u2013SUMO and Ubc9. Sumoylated proteins so obtained were affinity purified or isolated by immunoprecipitation. The isolated sumoylated proteins were identified by sequence analysis using mass spectrometric methods. Results reveal that several heterogeneous nuclear ribonucleoproteins (hnRNPs), zinc finger proteins, and nuclear pore complex proteins were sumoylated. The sumoylation of hnRNP A1, hnRNP F, and hnRNP K were confirmed\n            <jats:italic>in vivo</jats:italic>\n            by coimmunoprecipitation. In view of the facts that hnRNPs have been implicated in RNA splicing, transport, stability, and translation, our findings suggest that sumoylation could play an important role in regulating mRNA metabolism.\n          </jats:p>",
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