Regulation of Bcl-2 proteins during anoikis and amorphosis.
Adhesion to extracellular matrix regulates cell survival through both integrin engagement and appropriate cell spreading. Numerous signaling pathways converge to affect the levels and posttranslational modifications of Bcl-2 family proteins. Recent work has defined specific roles for different Bcl-2 proteins in the disruption of mitochondrial function that leads to cell death. Using this understanding of Bcl-2 protein function as a framework, we will consider the molecular mechanisms of apoptosis induced by integrin detachment (anoikis) and cell death stimulated by the loss of cytoskeletal architecture (amorphosis).
Martin
Stuart S
SS
Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur-NRB 356, Boston, MA 02115, USA. smartin@genetics.med.harvard.edu
Vuori
Kristiina
K
D000818:Animals; D023102:Anoikis / Q000502:physiology*; D051023:BH3 Interacting Domain Death Agonist Protein; D002352:Carrier Proteins / Q000378:metabolism; D003599:Cytoskeleton / Q000502:physiology*; D004789:Enzyme Activation; D006801:Humans; D016023:Integrins / Q000502:physiology*; D008928:Mitochondria / Q000502:physiology*; D010766:Phosphorylation; D017434:Protein Structure, Tertiary; D019253:Proto-Oncogene Proteins c-bcl-2 / Q000378:metabolism*; D018124:Receptors, Tumor Necrosis Factor / Q000378:metabolism; D053219:Receptors, Tumor Necrosis Factor, Member 25; D051028:bcl-2-Associated X Protein
D051023:BH3 Interacting Domain Death Agonist Protein; C494814:BID protein, human; D002352:Carrier Proteins; D016023:Integrins; D019253:Proto-Oncogene Proteins c-bcl-2; D018124:Receptors, Tumor Necrosis Factor; D053219:Receptors, Tumor Necrosis Factor, Member 25; C506033:TNFRSF25 protein, human; D051028:bcl-2-Associated X Protein