Programmed cell death during Caenorhabditis elegans development
Journal
Genetics
Journal Volume
203
Journal Issue
4
Pages
1533-1562
Date Issued
2016
Author(s)
Abstract
Programmed cell death is an integral component of Caenorhabditis elegans development. Genetic and reverse genetic studies in C. elegans have led to the identification of many genes and conserved cell death pathways that are important for the specification of which cells should live or die, the activation of the suicide program, and the dismantling and removal of dying cells. Molecular, cell biological, and biochemical studies have revealed the underlying mechanisms that control these three phases of programmed cell death. In particular, the interplay of transcriptional regulatory cascades and networks involving multiple transcriptional regulators is crucial in activating the expression of the key death-inducing gene egl-1 and, in some cases, the ced-3 gene in cells destined to die. A protein interaction cascade involving EGL-1, CED-9, CED-4, and CED-3 results in the activation of the key cell death protease CED-3, which is tightly controlled by multiple positive and negative regulators. The activation of the CED-3 caspase then initiates the cell disassembly process by cleaving and activating or inactivating crucial CED-3 substrates; leading to activation of multiple cell death execution events, including nuclear DNA fragmentation, mitochondrial elimination, phosphatidylserine externalization, inactivation of survival signals, and clearance of apoptotic cells. Further studies of programmed cell death in C. elegans will continue to advance our understanding of how programmed cell death is regulated, activated, and executed in general. ? 2016 by the Genetics Society of America.
Subjects
Activation phase; Caenorhabditis elegans; Execution phase; Programmed cell death; Specification phase; WormBook
SDGs
Other Subjects
ABL 1 protein; Caenorhabditis elegans protein; caspase; CED 1 protein; CED 12 protein; CED 3 protein; CED 5 protein; CED 6 protein; CED 7 protein; cell nucleus DNA; egl 1 protein; guanosine triphosphatase; lipid; MTM 1 protein; NSM protein; PAT 2 protein; PAT 3 protein; PDR 1 protein; PGRN 1 protein; phosphatidylserine; protein; proteinase; Rab protein; rid protein; SLI 1 protein; SRGP 1 protein; SWAN 1 protein; unclassified drug; Caenorhabditis elegans protein; calcium binding protein; caspase; ced-3 protein, C elegans; Ced-4 protein, C elegans; Ced-9 protein, C elegans; EGL-1 protein, C elegans; protein bcl 2; repressor protein; acidification; activation analysis; apoptosis; Article; asymmetric cell division; autophagy; biochemical analysis; Caenorhabditis elegans; cell activation; cell death; cell lineage; cell maturation; cell survival; clearance; companion cell; digestion; DNA degradation; DNA fragmentation; gene inactivation; genetic transcription; hermaphrodite; human; machine; mitochondrial membrane; nerve cell; nonhuman; phagocyte; phagosome; priority journal; protein degradation; protein expression; protein interaction; protein targeting; regulatory mechanism; second messenger; signal transduction; structure analysis; surface property; survival factor; animal; apoptosis; biosynthesis; Caenorhabditis elegans; gene expression regulation; gene regulatory network; genetics; growth, development and aging; Animals; Apoptosis; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Calcium-Binding Proteins; Caspases; DNA Fragmentation; Gene Expression Regulation, Developmental; Gene Regulatory Networks; Proto-Oncogene Proteins c-bcl-2; Repressor Proteins; Signal Transduction
Type
journal article