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BCL2 inhibits cell adhesion, spreading, and motility by enhancing actin polymerization.

dc.contributor.author Ke, Hengning
dc.contributor.author Parron, Vandy I
dc.contributor.author Reece, Jeff
dc.contributor.author Zhang, Jennifer Y
dc.contributor.author Akiyama, Steven K
dc.contributor.author French, John E
dc.coverage.spatial England
dc.date.accessioned 2017-08-02T14:10:41Z
dc.date.issued 2010-04
dc.identifier https://www.ncbi.nlm.nih.gov/pubmed/20142842
dc.identifier cr201021
dc.identifier.uri https://hdl.handle.net/10161/15167
dc.description.abstract BCL2 is best known as a multifunctional anti-apoptotic protein. However, little is known about its role in cell-adhesive and motility events. Here, we show that BCL2 may play a role in the regulation of cell adhesion, spreading, and motility. When BCL2 was overexpressed in cultured murine and human cell lines, cell spreading, adhesion, and motility were impaired. Consistent with these results, the loss of Bcl2 resulted in higher motility observed in Bcl2-null mouse embryonic fibroblast (MEF) cells compared to wild type. The mechanism of BCL2 regulation of cell adhesion and motility may involve formation of a complex containing BCL2, actin, and gelsolin, which appears to functionally decrease the severing activity of gelsolin. We have observed that the lysate from MCF-7 and NIH3T3 cells that overexpressed BCL2 enhanced actin polymerization in cell-free in vitro assays. Confocal immunofluorescent localization of BCL2 and F-actin during spreading consistently showed that increased expression of BCL2 resulted in increased F-actin polymerization. Thus, the formation of BCL2 and gelsolin complexes (which possibly contain other proteins) appears to play a critical role in the regulation of cell adhesion and migration. Given the established correlation of cell motility with cancer metastasis, this result may explain why the expression of BCL2 in some tumor cell types reduces the potential for metastasis and is associated with improved patient prognosis.
dc.language eng
dc.publisher Springer Science and Business Media LLC
dc.relation.ispartof Cell Res
dc.relation.isversionof 10.1038/cr.2010.21
dc.subject Actin Cytoskeleton
dc.subject Animals
dc.subject Cell Adhesion
dc.subject Cell Line, Tumor
dc.subject Cell Movement
dc.subject Gelsolin
dc.subject Humans
dc.subject Mice
dc.subject Mice, Knockout
dc.subject NIH 3T3 Cells
dc.subject Proto-Oncogene Proteins c-bcl-2
dc.title BCL2 inhibits cell adhesion, spreading, and motility by enhancing actin polymerization.
dc.type Journal article
duke.contributor.id Zhang, Jennifer Y|0380897
pubs.author-url https://www.ncbi.nlm.nih.gov/pubmed/20142842
pubs.begin-page 458
pubs.end-page 469
pubs.issue 4
pubs.organisational-group Clinical Science Departments
pubs.organisational-group Dermatology
pubs.organisational-group Duke
pubs.organisational-group Duke Cancer Institute
pubs.organisational-group Institutes and Centers
pubs.organisational-group Pathology
pubs.organisational-group School of Medicine
pubs.publication-status Published
pubs.volume 20
dc.identifier.eissn 1748-7838


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