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Is unconventional secretion inhibited during cell division by Cdk1 activity?
1Department of Biochemistry, Yong Loo Lin School of Medicine, National University Health System, NUS Graduate School of Integrative Sciences and Engineering, National University of Singapore, Singapore, Singapore. bchtbl@nus.edu.sg
Journal of Cellular Physiology
|October 23, 2012
Summary
Unconventional protein secretion, dependent on GRASP and autophagy, may be inhibited during cell division. This process bypasses the Golgi, but key proteins are phosphorylated by cyclin-dependent kinase 1 (Cdk1), potentially halting secretion.
Area of Science:
- Cell Biology
- Molecular Biology
- Protein Secretion
Background:
- Classical secretion is inhibited during cell division due to Golgi fragmentation.
- Unconventional secretion utilizes autophagy machinery and GRASP proteins.
- The impact of cell division on unconventional secretion remains unexplored.
Purpose of the Study:
- To investigate whether unconventional secretion is inhibited during cell division (mitosis).
- To explore the role of cell cycle regulation in unconventional secretion.
Main Methods:
- The study focuses on the known components of unconventional secretion, including GRASP and Vps34.
- It examines the phosphorylation of GRASP and Vps34 by cyclin-dependent kinase 1 (Cdk1) during the cell cycle.
Main Results:
- GRASP and Vps34 are identified as substrates of Cdk1.
- Cdk1 phosphorylation appears to inhibit the activity of GRASP and Vps34.
Conclusions:
- Unconventional secretion may be inhibited during cell division, similar to classical secretion.
- The cell cycle-dependent regulation of GRASP and Vps34 suggests a complex interplay between cell division and unconventional secretion.
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