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Updated: Jul 19, 2026
Use of Time-Lapse Microscopy and Stage-Specific Nuclear Depletion of Proteins to Study Meiosis in S. cerevisiae
Published on: October 11, 2022
XLX is an IAP family member regulated by phosphorylation during meiosis
1Integrated Program in Cellular, Molecular, and Biophysical Studies, Columbia University Medical Center, New York, NY 10032, USA.
Abstract:
The balance between proliferation and cell death is critical for embryonic development and adult tissue homeostasis. Within an individual cell, coordination of these pathways is aided by direct communication between cell cycle factors and molecules that regulate apoptosis. Here, we show that XLX, a Xenopus laevis inhibitor of apoptosis (IAP) family member, exhibits characteristics typical of an IAP, such as caspase inhibition and autoubiquitylation. However, unlike other IAPs described thus far, we found that XLX is phosphorylated during meiosis by protein kinases that belong to the MAPK and MPF pathways. Finally, we show that caspase-dependent cleavage of XLX is altered when XLX is phosphorylated. In addition to furthering our understanding of the post-translational regulation of an IAP, these findings reveal a novel link between cell cycle-regulated protein kinases and a component potentially involved in apoptosis.
Insights
Xenopus laevis inhibitor of apoptosis (IAP) XLX is phosphorylated during meiosis, altering its cleavage. This reveals a novel link between cell cycle kinases and apoptosis regulation.
Area of Science:
- Cell Biology
- Developmental Biology
- Molecular Biology
Background:
- The balance between cell proliferation and apoptosis is crucial for development and homeostasis.
- Cell cycle regulators and apoptosis molecules directly communicate to coordinate these processes within cells.
Purpose of the Study:
- To investigate the regulation and function of XLX, a Xenopus laevis inhibitor of apoptosis (IAP) family member.
- To explore the relationship between XLX phosphorylation, caspase-dependent cleavage, and cell cycle pathways.
Main Methods:
- Characterization of XLX protein properties, including caspase inhibition and autoubiquitylation.
- Analysis of XLX phosphorylation by MAPK and MPF pathways during meiosis.
- Assessment of how XLX phosphorylation affects its caspase-dependent cleavage.
Main Results:
- XLX exhibits typical IAP characteristics, including caspase inhibition and autoubiquitylation.
- XLX is phosphorylated by MAPK and MPF pathways during meiosis.
- Phosphorylation of XLX alters its caspase-dependent cleavage, indicating a novel regulatory mechanism.
Conclusions:
- XLX is a post-translationally regulated IAP involved in the interplay between cell cycle and apoptosis.
- Findings uncover a new connection between cell cycle-regulated kinases and apoptosis regulation in Xenopus laevis.
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