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© The Rockefeller University Press, 0021-9525/1997//759 $5.00
The Journal of Cell Biology, Volume 139, Number 3, , 1997 759-771

Article

Dismantling Cell–Cell Contacts during Apoptosis Is Coupled to a Caspase-dependent Proteolytic Cleavage of β-Catenin



Claudio Brancolini*,§, Dean Lazarevic*, Joe Rodriguez{ddagger}, and Claudio Schneider*,§

* Laboratorio Nazionale Consorzio Interuniversitario Biotecnologie AREA Science Park, 34142 Trieste, Italy; {ddagger} Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724; and § Dipartimento di Scienze e Tecnologie Biomediche, Sezione di Biologia, Universita' di Udine, 33100 Udine, Italy

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 cytoskeletal 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 {alpha}-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.

Abbreviations used in this paper: aa, amino acid; Gas, growth arrest specific protein; ICE, interleukin-1β–convertase enzyme; MMS, methylmethanesulfonate.

Address all correspondence to Claudio Schneider, Laboratorio Nazionale, Consorzio Interuniversitario Biotechnologie, AREA Science Park, Padriciano 99, 34142 Trieste, Italy. Tel.: 39.40.398.985. Fax: 39.40.398.990. E-mail: sch{at}icgeb.trieste.it


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