Proteomics studies of post-translational modifications in plants

Jae Kwon Sun, Young Choi Eun, Jung Choi Yoon, Hoon Ahn Ji, Ohkmae K. Park

Research output: Contribution to journalReview articlepeer-review

72 Citations (Scopus)


Post-translational modifications of proteins greatly increase protein complexity and dynamics, co-ordinating the intricate regulation of biological events. The global identification of post-translational modifications is a difficult task that is currently accelerated by advances in proteomics techniques. There has been significant development in sample preparation methods and mass spectrometry instrumentation. To reduce the complexity and to increase the amount of modified proteins available for analysis, proteins are usually subjected to prefractionation such as chromatographic purification and affinity enrichment. In this review, the post-translational modification studies in plants are summarized. The sample preparation strategies applied to each study are also described. These include affinity-based enrichment methods, immobilized metal affinity chromatography and immunoprecipitation used for phosphorylation and ubiquitination studies, respectively, and the phase partitioning approach for glycosylphosphatidylinositol modification studies.

Original languageEnglish
Pages (from-to)1547-1551
Number of pages5
JournalJournal of experimental botany
Issue number7
Publication statusPublished - 2006 Apr

Bibliographical note

Funding Information:
We acknowledge support from the Plant Signaling Network Research Center funded by the Korea Science and Engineering Foundation and the BioGreen 21 Program funded by the Rural Development Administration, Republic of Korea.


  • Glycosylphosphatidylinositol
  • Phosphorylation
  • Plant
  • Post-translational modification
  • Proteomics
  • Ubiquitination

ASJC Scopus subject areas

  • Physiology
  • Plant Science


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