SATB1 Cleavage by Caspase 6 Disrupts PDZ Domain-Mediated Dimerization, Causing Detachment from Chromatin Early in T-Cell Apoptosis

Galande, Sanjeev; Dickinson, Liliane A.; Mian, I. Saira; Sikorska, Marianna; Kohwi‐Shigematsu, Terumi

doi:10.1128/mcb.21.16.5591-5604.2001

Cited by 117 publications

(149 citation statements)

References 71 publications

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“…DNA from control and 2 h anti-Fas-treated (100 ng/ml) Jurkat cells was processed in agarose plugs and analysed by PFGE in a first dimension (a) and by CAGE in a second dimension (b), as described in the Materials and Methods section early in thymocyte apoptosis. 29 Here we report a similar phenomenon in anti-FAS-treated Jurkat cells ( Figure 3). In control cells, SATB1 immunostaining was pannucleoplasmic, excluded from nucleoli and confined within the nuclear interior defined by the lamin B staining (Figure 3a and b, lamin BFgreen, SATB1Fred).…”

Section: Alteration In Nuclear Satb1 Stainingsupporting

confidence: 60%

“…31 However, in many cell types undergoing apoptosis in response to a variety of agents, the degradation of nuclear matrix proteins, most notably those involved in the maintenance of normal chromatin structure, can be detected concurrently with HMW DNA cleavage and before ultimate nuclear collapse, 11,25,29,32 suggesting that these two degradative processes are interlinked. The data presented in this manuscript are consistent with this statement, since the proteolysis of NuMA, lamin B, PARP and SATB1 and the appearance of both ss and ds DNA breaks in anti-Fas-treated Jurkat cells were detected simultaneously and prior to the detectable loss of cell viability.…”

Section: Discussionmentioning

confidence: 99%

“…Typically, the BUR site of the IgH gene labelled a single protein of approximately 103 kDa, shown previously to be SATB1. 29 However, if the gels were subjected to a renaturation step in 4 M urea to remove SDS following the PAGE and prior to protein electrotransfer, not only was the binding of the probe to SATB1 more efficient, but an additional band of approximately 60 kDa was also clearly labelled by the probe (Figure 5c). The identity of this protein is unknown at present.…”

Section: Selection Of Genes Containing Bur-like Elementsmentioning

confidence: 99%

“…Although caspase-mediated proteolysis of these proteins during apoptosis has been previously reported, [8][9][10][11]29 this experiment was performed to compare their degradation kinetics with that of DNA. Activation of nuclear proteolysis was evident after 1 h of anti-Fas treatment (Figure 2, lamin B, NuMA).…”

Section: Temporal Correlation Between Nuclear Proteolysis and Endonucmentioning

confidence: 99%

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Mapping the initial DNA breaks in apoptotic Jurkat cells using ligation-mediated PCR

et al. 2003

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Apoptotic DNA degradation could be initiated by the accumulation of single-strand (ss) breaks in vulnerable chromatin regions, such as base unpairing regions (BURs), which might be preferentially targeted for degradation by both proteases and nucleases. We tested this hypothesis in antiFas-treated apoptotic Jurkat cells. Several nuclear proteins known for their association with both MARs and the nuclear matrix, that is, PARP, NuMA, lamin B and SATB1, were degraded, but the morphological rearrangement of the BURbinding SATB1 protein was one of the earliest detected changes. Subsequently, we have identified several genes containing sequences homologous to the 25 bp BUR element of the IgH gene, a known SATB1-binding site, and examined the integrity of genomic DNA in their vicinity. Multiple ss breaks were found in close proximity to these sites relative to adjacent regions of DNA. Consistent with our prediction, the results indicated that the initiation of DNA cleavage in antiFas-treated Jurkat cells occurred within the BUR sites, which likely became accessible to endonucleases due to the degradation of BUR-binding proteins.

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Section: Alteration In Nuclear Satb1 Stainingsupporting

confidence: 60%

Section: Discussionmentioning

confidence: 99%

Section: Selection Of Genes Containing Bur-like Elementsmentioning

confidence: 99%

Section: Temporal Correlation Between Nuclear Proteolysis and Endonucmentioning

confidence: 99%

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Mapping the initial DNA breaks in apoptotic Jurkat cells using ligation-mediated PCR

et al. 2003

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“…Caspase-6 cleaves several substrates including nuclear lamins, focal adhesion kinase, nuclear mitotic apparatus protein (NUMA) and the nuclear matrix protein, special AT-rich binding protein-1 (SATB1). [16][17][18][19] Most caspase-6 substrates, except for lamin A/C and SATB1, can be cleaved by other caspases. In the absence of caspase-6, cells with lamin A do not undergo complete nuclear condensation during the execution phase of apoptosis.…”

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confidence: 99%

Ordering of caspases in cells undergoing apoptosis by the intrinsic pathway

et al. 2009

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Caspases are a family of aspartate-specific cysteine proteases responsible for the biochemical and morphological changes that occur during the execution phase of apoptosis. The hierarchical ordering of caspases has been clearly established using dATPactivated cell lysates to model the intrinsic pathway induced by initial mitochondrial perturbation. In this model, caspase-9, the apical caspase, directly processes and activates the effector caspases, caspase-3 and -7, and then active caspase-3 but not caspase-7, processes caspase-2 and -6, and subsequently the activated caspase-6 processes caspase-8 and -10. To address the possibility that this model in vitro system might not reflect the precise ordering of caspases in intact cells, we have examined this possibility in cells induced to undergo apoptosis by activation of the intrinsic pathway. We have used caspase deficient cells, small interference RNA for caspase-6 and -7, and a specific caspase-3 inhibitor. In contrast to the earlier in vitro studies, we now show that in intact cells caspase-7 can also directly process and activate caspase-2 and -6. The processing of caspase-2 and -6 occurs within the cytoplasm and active caspase-6 is then responsible for both the processing of caspase-8 and the cleavage of caspase-6 substrates, including lamin A/C. Apoptosis, a major form of cell death used to remove unwanted or excess cells, is characterized by a plethora of morphological and biochemical changes resulting primarily from the activation of a family of cysteine proteases, which cleave their substrates at specific aspartate residues. 1-4 Two major apoptotic pathways have been described, the intrinsic pathway involving initial mitochondrial perturbation resulting from cellular stress or cytotoxic insults and the extrinsic pathway, which is triggered by the activation of death receptors of the TNF family. 5-7 Caspase-8 and -9, the apical caspases in the extrinsic and intrinsic pathways, possess a protein interaction prodomain, which result in their recruitment and subsequent activation within cellular complexes, namely the death-inducing signaling complex (DISC) and the Apaf-1 apoptosome, respectively, and the subsequent activation of effector caspases, such as caspase-3, -6 and -7. 5,[8][9][10] Caspases are synthesized as single-chain zymogens, containing an N-terminal prodomain, as well as large (B20 kDa) and small (B10 kDa) subunits, with the basic catalytic domain forming from a large and small subunits. 1,3,4 Caspase-2 also has a sizeable prodomain, but it is unclear whether it should be considered an initiator or an effector caspase. 3 Although caspase-2 has been proposed to act upstream of mitochondria and to be activated within the PIDDosome, it may also be activated downstream of caspase-3. 11-14 Using recombinant proteins, caspase-3, -8 and to a lesser extent caspase-7 can process caspase-2. 15 The physiological role of caspase-2 is not known and no marked phenotype is observed in caspase-2 À/À mice. Caspase-6 is generally considered to be an effector casp...

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Function of Proteins Identified as Part of the Nuclear Matrix

Zhang

Huo

Wen

2021

Encyclopedia of Life Sciences

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Nuclear matrix (NM) is an intranuclear protein network originally found after high‐salt or lithium diiodosalicylate extraction and nuclease treatment. Proteins identified as part of the NM comprise a multifunctional platform for various nuclear functions. NM contains proteins involved in chromatin packaging, deoxyribonucleic acid (DNA) replication, transcription, ribonucleic acid (RNA) splicing, DNA repair and cell signalling. Dysfunction of NM proteins may result in defective cell functions, abnormal organogenesis and disorders such as progeria and some cancers. Key Concepts Some NM proteins bind to chromatin via its scaffold/matrix‐attached regions (S/MARs), help chromatin loop formation or organise higher order chromatin architecture. The deoxyribonucleic acid (DNA) replication machinery can be attached to certain nuclear matrix (NM) proteins. Some NM proteins are associated with transcription factories and regulate gene expression. The abnormal expression or genetic variants of NM genes may cause development abnormalities and diseases.

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SATB1 Cleavage by Caspase 6 Disrupts PDZ Domain-Mediated Dimerization, Causing Detachment from Chromatin Early in T-Cell Apoptosis

Cited by 117 publications

References 71 publications

Mapping the initial DNA breaks in apoptotic Jurkat cells using ligation-mediated PCR

Mapping the initial DNA breaks in apoptotic Jurkat cells using ligation-mediated PCR

Ordering of caspases in cells undergoing apoptosis by the intrinsic pathway

Function of Proteins Identified as Part of the Nuclear Matrix

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