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pubmed-article:3350148pubmed:abstractTextThe tubulin molecule consists of an alpha- and a beta-subunit, each of which exists in several isotypic forms. It has been previously shown that one of the isotypes of neuroblastoma beta-tubulin is phosphorylated at a serine residue in vivo [(1985) J. Cell Biol. 100, 764-774]. Here we identify the phosphorylated isotype as beta 2 (type III). Moreover, the large size of the phosphorylated tryptic peptide and sequence comparisons of vertebrate beta-tubulins suggest that one of the two serines in positions 444 and 446 is the phosphorylated residue. Our results raise the possibility that beta 2-tubulin differs functionally from the other beta-tubulin isotypes.lld:pubmed
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pubmed-article:3350148pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:3350148pubmed:articleTitleIdentification of the phosphorylated beta-tubulin isotype in differentiated neuroblastoma cells.lld:pubmed
pubmed-article:3350148pubmed:affiliationDepartment of Biochemistry, University of Texas, San Antonio 78284.lld:pubmed
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