Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1988-5-11
pubmed:abstractText
The 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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
230
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
142-6
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Identification of the phosphorylated beta-tubulin isotype in differentiated neuroblastoma cells.
pubmed:affiliation
Department of Biochemistry, University of Texas, San Antonio 78284.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't