Association of a 14-3-3 protein with CMP-NeuAc:GM1 α2,3-Sialyltransferase

Luoyi Gao, Xin Bin Gu, David S. Yu, Robert K. Yu, Guichao Zeng

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


CMP-NeuAc:GM1 α2,3-sialyltransferase (ST-IV) was purified to homogeneity from rat brain. Microsequencing of the tryptic peptides derived from the purified enzyme revealed two amino acid sequences homologous to the 14-3-3 proteins. A polyclonal antibody was raised against purified ST-IV. A 33 kDa protein was co-immunoprecipitated from rat brain extracts with the anti-(ST-IV) antibody as detected by Western blot analysis. This protein was identified as a subtype of 14-3-3 family by an anti-(14-3-3) antibody. Screening of a rat brain λgt11 library using the anti-(ST-IV) antibody resulted in the identification of a cDNA clone coding for the subtype of 14-3-3 protein. These results indicate an association of the 14-3-3 protein with the sialyltransferase. Since the 14-3-3 protein has PKC inhibitor activities and the activity of sialyltransferases is, at least in part, regulated by PKC, the association of the 14-3-3 protein with ST-IV may indicate a role for this protein in the post-translational regulation of the sialyltransferase activity through the processes of phosphorylation and dephosphorylation.

Original languageEnglish (US)
Pages (from-to)103-107
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Jul 5 1996
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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