Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2006-5-15
pubmed:abstractText
Fesselin is an actin binding protein from smooth muscle that nucleates actin polymerization in a Ca(++)-calmodulin dependent manner, bundles actin and inhibits the actin-activated ATPase activity of myosin S1. We now report that fesselin binds to smooth muscle alpha-actinin. Binding was measured by blot overlay, affinity chromatography and sedimentation methods. Binding was moderate with an association constant of 1-4 x 10(7) M(-1) assuming a 1:1 association of fesselin with alpha-actinin. Fesselin binds to the central spectrin domain repeat region of alpha-actinin but not to the CH1-CH2 domain. Fesselin accelerates the polymerization of actin. This activity of fesselin was attenuated by alpha-actinin. These observations support the role of fesselin in organizing the cytoskeleton.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0142-4319
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
45-51
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Smooth muscle alpha-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization.
pubmed:affiliation
Brody School of Medicine at East Carolina University, 600 Moye Blvd., Greenville, NC 27834, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural