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 language | English (US) |
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Pages (from-to) | 142-146 |
Number of pages | 5 |
Journal | FEBS Letters |
Volume | 230 |
Issue number | 1-2 |
DOIs | |
State | Published - 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