Linked Life Data

20047880

Source:http://linkedlifedata.com/resource/pubmed/id/20047880

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-2-8
pubmed:abstractText
We isolated frizzy1 (fiz1), a novel dominant actin mutant from Arabidopsis. In the fiz1 mutant, Glu272 was substituted with lysine in the hydrophobic loop of ACT8, which is very important for the polymerization. Live imaging of actin filaments revealed that the fiz1 mutation induced fragmentation of actin filaments in a semi-dominant manner. In addition, the dynamics of Golgi stacks and mitochondria were disrupted by the fiz1 effects. From these results, it was strongly suggested that the fiz1 mutation had dominant-negative effects on actin polymerization, which causes defects in the functions of actin filaments such as organelle transport.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1471-9053
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
333-8
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Defects in dynamics and functions of actin filament in Arabidopsis caused by the dominant-negative actin fiz1-induced fragmentation of actin filament.
pubmed:affiliation
Graduate School of Biological Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma Nara, 630-0192 Japan.
pubmed:publicationType
Journal Article