Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-1-7
pubmed:abstractText
We have analyzed the detailed structure and cytoplasmic distribution of cytoplasmic microtubule-associated proteins. The procedure used to identify these proteins, based on preparation of detergent-extracted cytoskeletons, permits separation of fractions containing assembled and unassembled microtubule proteins. We show that two of these proteins, 69 and 80 kd, are closely related to one another and that each protein is present as a set of structurally related polypeptides with differing isoelectric points. In both neuroblastoma and pheochromocytoma cells, several of the isoelectric variants are greatly enriched in the fraction containing assembled microtubule components. Their differential distribution is correlated with phosphorylation at novel sites on the protein. These results support the possibility that covalent modification of a cytoskeletal component may specify its functional state.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
407-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Cytoplasmic microtubule-associated proteins: phosphorylation at novel sites is correlated with their incorporation into assembled microtubules.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.