Linked Life Data

10327055

Source:http://linkedlifedata.com/resource/pubmed/id/10327055

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1999-6-3
pubmed:abstractText
Nuclear localization of p53 is required for p53 to detect and respond to DNA strand abnormalities and breaks following DNA damage. This leads to activation of the tumour suppressive functions of p53 resulting in either cell cycle arrest and DNA repair; or apoptosis. Critical functional changes in DNA which require strand breaks, including gene rearrangement, may transiently mimic DNA damage: here it is important not to trigger a p53 response. The fine control of p53 in these different circumstances is unknown but may include transient sequestering of p53 in the cytoplasm. Reversible nuclear-cytoplasmic shuttling is an intrinsic property of p53 (Middeler et al., 1997) associated with cell cycle-related changes in p53's subcellular distribution. Takahashi and Suzuki (1994) described p53 inactivation by shuttling to the cytoplasm and Katsumoto et al. (1995) found wild-type p53 to be closely associated with cytoplasmic actin filaments during DNA synthesis. Here we show that, in the presence of free calcium ions, p53 binds directly to F-actin with a dissocation constant of about 10 microM. Thus, part of the regulatory machinery in normal cell cycling may involve p53-actin interactions regulated by calcium fluxes and the dynamic turnover of F-actin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0950-9232
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2351-5
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Wild-type p53 protein shows calcium-dependent binding to F-actin.
pubmed:affiliation
Department of Surgery, Addenbrookes Hospital, Cambridge, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't