ArticleThe Biochemical journal2004
AlphaII-spectrin is an in vitro target for caspase-2, and its cleavage is regulated by calmodulin binding.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 64 citations in OpenAlex.
- Critical role of alpha spectrin in DNA repair: the importance of μ-calpain and Fanconi anemia proteins.Experimental biology and medicine (Maywood, N.J.) · 2025Review
- Article
- The Role of Caspase-2 in Regulating Cell Fate.Cells · 2020Review
- Human erythrocytes: cytoskeleton and its origin.Cellular and molecular life sciences : CMLS · 2020Review
- The functional importance of lamins, actin, myosin, spectrin and the LINC complex in DNA repair.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- The role of spectrin in cell adhesion and cell-cell contact.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- The Spectrinome: The Interactome of a Scaffold Protein Creating Nuclear and Cytoplasmic Connectivity and Function.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- The Role of Nonerythroid SpectrinJournal of oncology · 2019Review
- Spectrin and its interacting partners in nuclear structure and function.Experimental biology and medicine (Maywood, N.J.) · 2018Review
- Influence of Membrane Receptor Lateral Diffusion on the Short-Term Depression of Acetylcholine-Induced Current in Helix Neurons.Cellular and molecular neurobiology · 2017Article
- Spectrin and phospholipids - the current picture of their fascinating interplay.Cellular & molecular biology letters · 2014Review
- Caspase-2 promotes cytoskeleton protein degradation during apoptotic cell death.Cell death & disease · 2013Article
- Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown.Brain research · 2013Article
- Caspase-2 short isoform interacts with membrane-associated cytoskeleton proteins to inhibit apoptosis.PloS one · 2013Article
- Chemosensitivity is controlled by p63 modification with ubiquitin-like protein ISG15.The Journal of clinical investigation · 2012Article
- Spectrin-based skeleton as an actor in cell signaling.Cellular and molecular life sciences : CMLS · 2012Review
- Mice lacking caspase-2 are protected from behavioral changes, but not pathology, in the YAC128 model of Huntington disease.Molecular neurodegeneration · 2011Article
- Aggregation of spectrin and PKCtheta is an early hallmark of fludarabine/mitoxantrone/dexamethasone-induced apoptosis in Jurkat T and HL60 cells.Molecular and cellular biochemistry · 2010Article
- DNA-PKcs-PIDDosome: a nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance.Cell · 2009Article
- The enigma of caspase-2: the laymen's view.Cell death and differentiation · 2009Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The spectrin-actin scaffold underlying the lipid bilayer is considered to participate in cell-shape stabilization and in the organization of specialized membrane subdomains. These structures are dynamic and likely to undergo frequent remodelling during changes in cell shape. Proteolysis of spectrin, which occurs during apoptosis, leads to destabilization of the scaffold. It is also one of the major processes involved in membrane remodelling. Spectrins, the main components of the membrane skeleton, are the targets for two important protease systems: m- and micro-calpains (Ca2+-activated proteases) and caspase-3 (activated during apoptosis). In this paper, we show that caspase-2 also targets spectrin in vitro, and we characterize Ca2+/calmodulin-dependent regulation of spectrin cleavage by caspases. Yeast two-hybrid screening reveals that the large isoform (1/L) of procaspase-2 specifically binds to alphaII-spectrin, while the short isoform does not. Like caspase-3, caspase-2 cleaves alphaII-spectrin in vitro at residue Asp-1185. This study emphasizes a role of executioner caspase for caspase-2. We also demonstrated that the executioner caspase-7 but not caspase-6 cleaves spectrin at residue Asp-1185 in vitro. This spectrin cleavage by caspases 2, 3 and 7 is inhibited by the Ca2+-dependent binding of calmodulin to spectrin. In contrast, calmodulin binding enhances spectrin cleavage by calpain at residue Tyr-1176. These results indicate that alphaII-spectrin cleavage is highly influenced by Ca2+ homoeostasis and calmodulin, which therefore represent potential regulators of the stability and the plasticity of the spectrin-based skeleton.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.