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Journal article
Ack kinase regulates CTP synthase filaments during Drosophila oogenesis
EMBO reports, v 15(11), pp 1184-1191
Nov 2014
PMID: 25223282
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
The enzyme CTP synthase (CTPS) dynamically assembles into macromolecular filaments in bacteria, yeast, Drosophila, and mammalian cells, but the role of this morphological reorganization in regulating CTPS activity is controversial. During Drosophila oogenesis, CTPS filaments are transiently apparent in ovarian germline cells during a period of intense genomic endoreplication and stockpiling of ribosomal RNA. Here, we demonstrate that CTPS filaments are catalytically active and that their assembly is regulated by the non-receptor tyrosine kinase DAck, the Drosophila homologue of mammalian Ack1 (activated cdc42-associated kinase 1), which we find also localizes to CTPS filaments. Egg chambers from flies deficient in DAck or lacking DAck catalytic activity exhibit disrupted CTPS filament architecture and morphological defects that correlate with reduced fertility. Furthermore, ovaries from these flies exhibit reduced levels of total RNA, suggesting that DAck may regulate CTP synthase activity. These findings highlight an unexpected function for DAck and provide insight into a novel pathway for the developmental control of an essential metabolic pathway governing nucleotide biosynthesis.
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Details
- Title
- Ack kinase regulates CTP synthase filaments during Drosophila oogenesis
- Creators
- Todd I Strochlic - Fox Chase Cancer CenterKevin P Stavrides - Fox Chase Cancer CenterSam V Thomas - Fox Chase Cancer CenterEmmanuelle Nicolas - Fox Chase Cancer CenterAlana M O'Reilly - Cancer Biology Program, Fox Chase Cancer Center, Philadelphia, PA, USA Epigenetics and Progenitor Cells Keystone Program, Fox Chase Cancer Center, Philadelphia, PA, USA Todd.Strochlic@drexelmed.edu Alana.OReilly@fccc.edu jeffrey.peterson@fccc.eduJeffrey R Peterson - Fox Chase Cancer Center
- Publication Details
- EMBO reports, v 15(11), pp 1184-1191
- Publisher
- EMBO Press
- Grant note
- P30 CA006927 / NCI NIH HHS R01 GM083025 / NIGMS NIH HHS R01 HD065800 / NICHD NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000344795500014
- Scopus ID
- 2-s2.0-84910125140
- Other Identifier
- 991019167317504721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Cell Biology