Abstract
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).
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, P.H.S.
-
Review
MeSH terms
-
Animals
-
Anoikis / physiology*
-
BH3 Interacting Domain Death Agonist Protein
-
Carrier Proteins / metabolism
-
Cytoskeleton / physiology*
-
Enzyme Activation
-
Humans
-
Integrins / physiology*
-
Mitochondria / physiology*
-
Phosphorylation
-
Protein Structure, Tertiary
-
Proto-Oncogene Proteins c-bcl-2 / metabolism*
-
Receptors, Tumor Necrosis Factor / metabolism
-
Receptors, Tumor Necrosis Factor, Member 25
-
bcl-2-Associated X Protein
Substances
-
BH3 Interacting Domain Death Agonist Protein
-
BID protein, human
-
Carrier Proteins
-
Integrins
-
Proto-Oncogene Proteins c-bcl-2
-
Receptors, Tumor Necrosis Factor
-
Receptors, Tumor Necrosis Factor, Member 25
-
TNFRSF25 protein, human
-
bcl-2-Associated X Protein