NPP-16/Nup50 function and CDK-1 inactivation are associated with anoxia-induced prophase arrest in Caenorhabditis elegans.
Oxygen, an essential nutrient, is sensed by a multiple of cellular pathways that facilitate the responses to and survival of oxygen deprivation. The Caenorhabditis elegans embryo exposed to severe oxygen deprivation (anoxia) enters a state of suspended animation in which cell cycle progression reversibly arrests at specific stages. The mechanisms regulating interphase, prophase, or metaphase arrest in response to anoxia are not completely understood. Characteristics of arrested prophase blastomeres and oocytes are the alignment of condensed chromosomes at the nuclear periphery and an arrest of nuclear envelope breakdown. Notably, anoxia-induced prophase arrest is suppressed in mutant embryos lacking nucleoporin NPP-16/NUP50 function, indicating that this nucleoporin plays an important role in prophase arrest in wild-type embryos. Although the inactive form of cyclin-dependent kinase (CDK-1) is detected in wild-type-arrested prophase blastomeres, the inactive state is not detected in the anoxia exposed npp-16 mutant. Furthermore, we found that CDK-1 localizes near chromosomes in anoxia-exposed embryos. These data support the notion that NPP-16 and CDK-1 function to arrest prophase blastomeres in C. elegans embryos. The anoxia-induced shift of cells from an actively dividing state to an arrested state reveals a previously uncharacterized prophase checkpoint in the C. elegans embryo.
Hajeri
Vinita A
VA
Department of Biological Sciences, University of North Texas, Denton, TX 76203, USA.
Little
Brent A
BA
Ladage
Mary L
ML
Padilla
Pamela A
PA
D000818:Animals; D001755:Blastocyst / Q000378:metabolism*; D016203:CDC2 Protein Kinase / Q000378:metabolism*; D017173:Caenorhabditis elegans / Q000235:genetics* / Q000502:physiology; D029742:Caenorhabditis elegans Proteins / Q000235:genetics* / Q000502:physiology; D005260:Female; D019084:Fluorescent Antibody Technique, Indirect; D005786:Gene Expression Regulation; D000860:Hypoxia; D009154:Mutation; D015739:Nocodazole / Q000494:pharmacology; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry / Q000235:genetics* / Q000502:physiology; D009687:Nuclear Proteins / Q000502:physiology*; D009865:Oocytes / Q000378:metabolism; D011418:Prophase; D034622:RNA Interference
D029742:Caenorhabditis elegans Proteins; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; C550136:npp-16 protein, C elegans; D016203:CDC2 Protein Kinase; D015739:Nocodazole