Linked Life Data

9865614

Source:http://linkedlifedata.com/resource/pubmed/id/9865614

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1999-3-5
pubmed:abstractText
Phosphorylation, dimerization and binding to calmodulin have been reported to influence the microtubule assembly capacities of MAPs (microtubule-associated proteins). Here we report that the Drosophila 205K MAP is a phosphoprotein in vivo and can be phosphorylated by cdc2/p34 in vitro. Bacterially produced 205K MAP is competent of microtubule assembly and microtubule bundling and binds to immobilized calmodulin in a Ca2+-dependent way. EM rotary shadowing analyses suggest that 205K MAP consists of an amino-terminal flexible extended region and a carboxy-terminal globular domain. This carboxy-terminal region harbors the microtubule binding site and sequences required for dimerization, as confirmed by in vitro crosslinking experiments of truncated proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
379
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1381-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Analysis of structure and microtubule assembly activity of the Drosophila 205K MAP.
pubmed:affiliation
Division of Oncology, University of Geneva Medical Center, Switzerland.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't