Abstract
Apoptosis of Jurkat T cells induced the caspase-mediated proteolytic cleavage of p21-activated kinase 2 (PAK2). Cleavage occurred between the amino-terminal regulatory domain and the carboxyl-terminal catalytic domain, which generated a constitutively active PAK2 fragment. Stable Jurkat cell lines that expressed a dominant-negative PAK mutant were resistant to the Fas-induced formation of apoptotic bodies, but had an enhanced externalization of phosphatidylserine at the cell surface. Thus, proteolytic activation of PAK2 represents a guanosine triphosphatase–independent mechanism of PAK regulation that allows PAK2 to regulate morphological changes that are seen in apoptotic cells.
Keywords
Jurkat cellsPhosphatidylserineCell biologyApoptosisCleavage (geology)GuanosineCaspaseKinaseChemistryBiologyBiochemistryProgrammed cell deathMembraneT cell
Affiliated Institutions
Related Publications
Cleavage of Focal Adhesion Kinase by Caspases during Apoptosis
Apoptotic cells undergo characteristic morphological changes that include detachment of cell attachment from the substratum and loss of cell-cell interactions. Attachment of cel...
Conversion of Bcl-2 to a Bax-like Death Effector by Caspases
Caspases are a family of cysteine proteases implicated in the biochemical and morphological changes that occur during apoptosis (programmed cell death). The loop domain of Bcl-2...
Autoproteolytic Activation of Pro-Caspases by Oligomerization
Initiation of apopotosis requires the conversion of procaspases to mature caspases. Here we show that oligomerization of pro-caspases is sufficient to induce proteolytic generat...
The gasdermins, a protein family executing cell death and inflammation
The gasdermins are a family of recently identified pore-forming effector proteins that cause membrane permeabilization and pyroptosis, a lytic pro-inflammatory type of cell deat...
Caspase Activation Involves the Formation of the Aposome, a Large (∼700 kDa) Caspase-activating Complex
In mammals, apoptotic protease-activating factor 1 (Apaf-1), cytochrome c, and dATP activate caspase-9, which initiates the postmitochondrial-mediated caspase cascade by proteol...
Publication Info
- Year
- 1997
- Type
- article
- Volume
- 276
- Issue
- 5318
- Pages
- 1571-1574
- Citations
- 743
- Access
- Closed
External Links
Social Impact
Altmetric
PlumX Metrics
Social media, news, blog, policy document mentions
Citation Metrics
743
OpenAlex
Cite This
Thomas Rudel,
Gary Bokoch
(1997).
Membrane and Morphological Changes in Apoptotic Cells Regulated by Caspase-Mediated Activation of PAK2.
Science
, 276
(5318)
, 1571-1574.
https://doi.org/10.1126/science.276.5318.1571
Identifiers
- DOI
- 10.1126/science.276.5318.1571