Linked Life Data

16428310

Source:http://linkedlifedata.com/resource/pubmed/id/16428310

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2006-1-23
pubmed:abstractText
We previously reported that caldesmon (CaD), together with tropomyosin (TM), effectively protects actin filaments from gelsolin, an actin-severing protein. To elucidate the structure/function relationship of CaD, we dissected the functional domain of CaD required for the protection. The basic C-terminal half of rat nonmuscle CaD (D3) inhibits gelsolin activity to the same degree as intact CaD, although a smaller C-terminal region of D3 does not. This smaller C-terminal region contains the minimum regulatory domain responsible for the inhibition of actomyosin ATPase, and for the binding to actin, calmodulin and TM. These results suggest that the domain responsible for the inhibition of gelsolin activity lies outside the minimum regulatory domain, and that the positive charge possessed by the C-terminal half of CaD is important for its interaction with actin. Moreover, while the D3 fragment promotes the aggregation of F-actin into bundles as reported previously, this bundle formation is inhibited by the acidic N-terminal half of CaD, as well as by poly-l-glutamate. It seems likely that the acidic N-terminal half of CaD neutralizes the superfluous basic feature of the C-terminal half. A comparison between D3 and calponin, another actin-binding protein that is also basic and has similar actin-regulatory activities, is also discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1756-2651
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
138
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
805-13
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Role of the basic C-terminal half of caldesmon in its regulation of F-actin: comparison between caldesmon and calponin.
pubmed:affiliation
Department of Molecular Biology and Biochemistry, Nelson Labs/Busch Campus, Rutgers, The State University of New Jersey, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, N.I.H., Extramural