Par-4-mediated recruitment of Amida to the actin cytoskeleton leads to the induction of apoptosis. Export

@article{citeulike:784519, abstract = {Par-4 (prostate apoptosis response-4) sensitizes cells to apoptotic stimuli, but the exact mechanisms are still poorly understood. Using Par-4 as bait in a yeast two-hybrid screen, we identified Amida as a novel interaction partner, a ubiquitously expressed protein which has been suggested to be involved in apoptotic processes. Complex formation of Par-4 and Amida occurs in vitro and in vivo and is mediated via the C-termini of both proteins, involving the leucine zipper of Par-4. Amida resides mainly in the nucleus but displays nucleo-cytoplasmic shuttling in heterokaryons. Upon coexpression with Par-4 in REF52.2 cells, Amida translocates to the cytoplasm and is recruited to actin filaments by Par-4, resulting in enhanced induction of apoptosis. The synergistic effect of Amida/Par-4 complexes on the induction of apoptosis is abrogated when either Amida/Par-4 complex formation or association of these complexes with the actin cytoskeleton is impaired, indicating that the Par-4-mediated relocation of Amida to the actin cytoskeleton is crucial for the pro-apoptotic function of Par-4/Amida complexes in REF52.2 cells. The latter results in enhanced phosphorylation of the regulatory light chain of myosin II (MLC) as has previously been shown for Par-4-mediated recruitment of DAP-like kinase (Dlk), suggesting that the recruitment of nuclear proteins involved in the regulation of apoptotic processes to the actin filament system by Par-4 represents a potent mechanism how Par-4 can trigger apoptosis.}, address = {Institute of Genetics, University of Bonn, R\"{o}merstr. 164, D-53117 Bonn, Germany.}, author = {Boosen, M. and Vetterkind, S. and Koplin, A. and Illenberger, S. and Preuss, U.}, citeulike-article-id = {784519}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.yexcr.2005.09.010}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16229834}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16229834}, day = {10}, doi = {10.1016/j.yexcr.2005.09.010}, issn = {0014-4827}, journal = {Exp Cell Res}, keywords = {amida, arc}, month = {December}, number = {2}, pages = {177--191}, posted-at = {2006-08-03 14:15:09}, priority = {2}, title = {Par-4-mediated recruitment of Amida to the actin cytoskeleton leads to the induction of apoptosis.}, url = {http://dx.doi.org/10.1016/j.yexcr.2005.09.010}, volume = {311}, year = {2005} }

TY - JOUR ID - citeulike:784519 L3 - citeulike-article-id:784519 N2 - Par-4 (prostate apoptosis response-4) sensitizes cells to apoptotic stimuli, but the exact mechanisms are still poorly understood. Using Par-4 as bait in a yeast two-hybrid screen, we identified Amida as a novel interaction partner, a ubiquitously expressed protein which has been suggested to be involved in apoptotic processes. Complex formation of Par-4 and Amida occurs in vitro and in vivo and is mediated via the C-termini of both proteins, involving the leucine zipper of Par-4. Amida resides mainly in the nucleus but displays nucleo-cytoplasmic shuttling in heterokaryons. Upon coexpression with Par-4 in REF52.2 cells, Amida translocates to the cytoplasm and is recruited to actin filaments by Par-4, resulting in enhanced induction of apoptosis. The synergistic effect of Amida/Par-4 complexes on the induction of apoptosis is abrogated when either Amida/Par-4 complex formation or association of these complexes with the actin cytoskeleton is impaired, indicating that the Par-4-mediated relocation of Amida to the actin cytoskeleton is crucial for the pro-apoptotic function of Par-4/Amida complexes in REF52.2 cells. The latter results in enhanced phosphorylation of the regulatory light chain of myosin II (MLC) as has previously been shown for Par-4-mediated recruitment of DAP-like kinase (Dlk), suggesting that the recruitment of nuclear proteins involved in the regulation of apoptotic processes to the actin filament system by Par-4 represents a potent mechanism how Par-4 can trigger apoptosis. IS - 2 JF - Exp Cell Res SN - 0014-4827 AD - Institute of Genetics, University of Bonn, Römerstr. 164, D-53117 Bonn, Germany. EP - 191 TI - Par-4-mediated recruitment of Amida to the actin cytoskeleton leads to the induction of apoptosis. VL - 311 SP - 177 KW - amida KW - arc AU - Boosen, M AU - Vetterkind, S AU - Koplin, A AU - Illenberger, S AU - Preuss, U PY - 2005/12/10/ UR - http://dx.doi.org/10.1016/j.yexcr.2005.09.010 ER -