Matches in UGent Biblio for { <https://biblio.ugent.be/publication/778394#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B417079.
- aggregation creator B417080.
- aggregation creator B417081.
- aggregation creator B417082.
- aggregation creator B417083.
- aggregation creator B417084.
- aggregation creator B417085.
- aggregation creator B417086.
- aggregation creator B417087.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2009".
- aggregation format "application/pdf".
- aggregation hasFormat 778394.bibtex.
- aggregation hasFormat 778394.csv.
- aggregation hasFormat 778394.dc.
- aggregation hasFormat 778394.didl.
- aggregation hasFormat 778394.doc.
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- aggregation hasFormat 778394.yaml.
- aggregation isPartOf urn:issn:1059-1524.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Unbalancing the phosphatidylinositol-4,5-bisphosphate-cofilin interaction impairs cell steering".
- aggregation abstract "Cofilin is a key player in actin dynamics during cell migration. Its activity is regulated by ( de) phosphorylation, pH, and binding to phosphatidylinositol-4,5-bisphosphate [PI(4,5)P(2)]. Here, we here use a human cofilin-1 (D122K) mutant with increased binding affinity for PI(4,5)P(2) and slower release from the plasma membrane to study the role of the PI(4,5)P(2)-cofilin interaction in migrating cells. In fibroblasts in a background of endogenous cofilin, D122K cofilin expression negatively affects cell turning frequency. In carcinoma cells with down-regulated endogenous cofilin, D122K cofilin neither rescues the drastic morphological defects nor restores the effects in cell turning capacity, unlike what has been reported for wild-type cofilin. In cofilin knockdown cells, D122K cofilin expression promotes outgrowth of an existing lamellipod in response to epidermal growth factor (EGF) but does not result in initiation of new lamellipodia. This indicates that, next to phospho- and pH regulation, the normal release kinetics of cofilin from PI(4,5)P(2) is crucial as a local activation switch for lamellipodia initiation and as a signal for migrating cells to change direction in response to external stimuli. Our results demonstrate that the PI(4,5)P(2) regulatory mechanism, that is governed by EGF-dependent phospholipase C activation, is a determinant for the spatial and temporal control of cofilin activation required for lamellipodia initiation.".
- aggregation authorList BK737268.
- aggregation endPage "4523".
- aggregation issue "21".
- aggregation startPage "4509".
- aggregation volume "20".
- aggregation aggregates 3039930.
- aggregation isDescribedBy 778394.
- aggregation similarTo mbc.E09-02-0121.
- aggregation similarTo LU-778394.