Identification of the phosphorylated β-tubulin isotype in differentiated neuroblastoma cells

Richard F. Ludueña, Hans Peter Zimmermann, Melvyn Little

Research output: Contribution to journalArticlepeer-review

57 Scopus citations

Abstract

The tubulin molecule consists of an α- and a β-subunit, each of which exists in several isotypic forms. It has been previously shown that one of the isotypes of neuroblastoma β-tubulin is phosphorylated at a serine residue in vivo [(1985) J. Cell Biol. 100, 764-774]. Here we identify the phosphorylated isotype as β2 (type III). Moreover, the large size of the phosphorylated tryptic peptide and sequence comparisons of vertebrate β-tubulins suggest that one of the two serines in positions 444 and 446 is the phosphorylated residue. Our results raise the possibility that β2-tubulin differs functionally from the other β-tubulin isotypes.

Original languageEnglish (US)
Pages (from-to)142-146
Number of pages5
JournalFEBS Letters
Volume230
Issue number1-2
DOIs
StatePublished - Mar 28 1988

Keywords

  • Neuroblastoma tubulin
  • Tubulin isotype
  • Tubulin phosphorylation
  • β-Tubulin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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