Abstract
Cell death by apoptosis is a tightly regulated process that requires coordinated modification in cellular architecture. The caspase protease family has been shown to play a key role in apoptosis. Here we report that specific and ordered changes in the actin cytoskeleton take place during apoptosis. In this context, we have dissected one of the first hallmarks in cell death, represented by the severing of contacts among neighboring cells. More specifically, we provide demonstration for the mechanism that could contribute to the disassembly of cytosketetal organization at cell-cell adhesion. In fact, β-catenin, a known regulator of cell-cell adhesion, is proteolytically processed in different cell types after induction of apoptosis. Caspase-3 (cpp32/apopain/yama) cleaves in vitro translated β- catenin into a form which is similar in size to that observed in cells undergoing apoptosis. β-Catenin cleavage, during apoptosis in vivo and after caspase-3 treatment in vitro, removes the amino- and carboxy-terminal regions of the protein. The resulting β-catenin product is unable to bind α- catenin that is responsible for actin filament binding and organization. This evidence indicates that connection with actin filaments organized at cell- cell contacts could be dismantled during apoptosis. Our observations suggest that caspases orchestrate the specific and sequential changes in the actin cytoskeleton occurring during cell death via cleavage of different regulators of the microfilament system.
| Original language | English |
|---|---|
| Pages (from-to) | 759-771 |
| Number of pages | 13 |
| Journal | Journal of Cell Biology |
| Volume | 139 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Nov 3 1997 |
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ASJC Scopus subject areas
- Cell Biology
Cite this
Dismantling cell-cell contacts during apoptosis is coupled to a caspase- dependent proteolytic cleavage of β-catenin. / Brancolini, Claudio; Lazarevic, Dean; Rodriguez, Joe; Schneider, Claudio.
In: Journal of Cell Biology, Vol. 139, No. 3, 03.11.1997, p. 759-771.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Dismantling cell-cell contacts during apoptosis is coupled to a caspase- dependent proteolytic cleavage of β-catenin
AU - Brancolini, Claudio
AU - Lazarevic, Dean
AU - Rodriguez, Joe
AU - Schneider, Claudio
PY - 1997/11/3
Y1 - 1997/11/3
N2 - Cell death by apoptosis is a tightly regulated process that requires coordinated modification in cellular architecture. The caspase protease family has been shown to play a key role in apoptosis. Here we report that specific and ordered changes in the actin cytoskeleton take place during apoptosis. In this context, we have dissected one of the first hallmarks in cell death, represented by the severing of contacts among neighboring cells. More specifically, we provide demonstration for the mechanism that could contribute to the disassembly of cytosketetal organization at cell-cell adhesion. In fact, β-catenin, a known regulator of cell-cell adhesion, is proteolytically processed in different cell types after induction of apoptosis. Caspase-3 (cpp32/apopain/yama) cleaves in vitro translated β- catenin into a form which is similar in size to that observed in cells undergoing apoptosis. β-Catenin cleavage, during apoptosis in vivo and after caspase-3 treatment in vitro, removes the amino- and carboxy-terminal regions of the protein. The resulting β-catenin product is unable to bind α- catenin that is responsible for actin filament binding and organization. This evidence indicates that connection with actin filaments organized at cell- cell contacts could be dismantled during apoptosis. Our observations suggest that caspases orchestrate the specific and sequential changes in the actin cytoskeleton occurring during cell death via cleavage of different regulators of the microfilament system.
AB - Cell death by apoptosis is a tightly regulated process that requires coordinated modification in cellular architecture. The caspase protease family has been shown to play a key role in apoptosis. Here we report that specific and ordered changes in the actin cytoskeleton take place during apoptosis. In this context, we have dissected one of the first hallmarks in cell death, represented by the severing of contacts among neighboring cells. More specifically, we provide demonstration for the mechanism that could contribute to the disassembly of cytosketetal organization at cell-cell adhesion. In fact, β-catenin, a known regulator of cell-cell adhesion, is proteolytically processed in different cell types after induction of apoptosis. Caspase-3 (cpp32/apopain/yama) cleaves in vitro translated β- catenin into a form which is similar in size to that observed in cells undergoing apoptosis. β-Catenin cleavage, during apoptosis in vivo and after caspase-3 treatment in vitro, removes the amino- and carboxy-terminal regions of the protein. The resulting β-catenin product is unable to bind α- catenin that is responsible for actin filament binding and organization. This evidence indicates that connection with actin filaments organized at cell- cell contacts could be dismantled during apoptosis. Our observations suggest that caspases orchestrate the specific and sequential changes in the actin cytoskeleton occurring during cell death via cleavage of different regulators of the microfilament system.
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UR - http://www.scopus.com/inward/citedby.url?scp=0030707519&partnerID=8YFLogxK
U2 - 10.1083/jcb.139.3.759
DO - 10.1083/jcb.139.3.759
M3 - Article
C2 - 9348292
AN - SCOPUS:0030707519
VL - 139
SP - 759
EP - 771
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 3
ER -