Related Experiment Video
Updated: Apr 1, 2026

Methods to Classify Cytoplasmic Foci as Mammalian Stress Granules
Published on: May 12, 2017
Syk Is Recruited to Stress Granules and Promotes Their Clearance through Autophagy
Mariya O Krisenko1, Reneé L Higgins1, Soumitra Ghosh1
1From the Department of Medicinal Chemistry and Molecular Pharmacology and the Purdue Center for Cancer Research, Purdue University, West Lafayette, Indiana 47907.
Abstract:
Syk is a cytoplasmic kinase that serves multiple functions within the immune system to couple receptors for antigens and antigen-antibody complexes to adaptive and innate immune responses. Recent studies have identified additional roles for the kinase in cancer cells, where its expression can either promote or suppress tumor cell growth, depending on the context. Proteomic analyses of Syk-binding proteins identified several interacting partners also found to be recruited to stress granules. We show here that the treatment of cells with inducers of stress granule formation leads to the recruitment of Syk to these protein-RNA complexes. This recruitment requires the phosphorylation of Syk on tyrosine and results in the phosphorylation of proteins at or near the stress granule. Grb7 is identified as a Syk-binding protein involved in the recruitment of Syk to the stress granule. This recruitment promotes the formation of autophagosomes and the clearance of stress granules from the cell once the stress is relieved, enhancing the ability of cells to survive the stress stimulus.
Insights
Spleen tyrosine kinase (Syk) is recruited to cellular stress granules, promoting cell survival. This process involves Syk phosphorylation and interactions with Grb7, aiding in stress granule clearance via autophagy.
Area of Science:
- Cell Biology
- Immunology
- Cancer Biology
Background:
- Spleen tyrosine kinase (Syk) is crucial for immune responses.
- Syk also plays a context-dependent role in cancer cell growth.
- Syk interacts with proteins found in stress granules.
Purpose of the Study:
- To investigate the role of Syk in cellular stress granules.
- To identify mechanisms of Syk recruitment to stress granules.
- To understand how Syk influences cellular stress response and survival.
Main Methods:
- Proteomic analysis to identify Syk-binding proteins.
- Cellular treatments with stress granule inducers.
- Phosphorylation site analysis of Syk.
- Immunofluorescence and autophagy assays.
Main Results:
- Syk is recruited to stress granules upon cellular stress.
- Syk recruitment requires tyrosine phosphorylation and involves Grb7.
- Recruited Syk phosphorylates nearby proteins and promotes autophagosome formation.
- Stress granule clearance and enhanced cell survival are observed.
Conclusions:
- Syk plays a novel role in the cellular stress response.
- Syk's localization to stress granules is a regulated process.
- Syk contributes to cell survival by facilitating stress granule resolution through autophagy.
Related Concept Videos
Autophagy
An autophagic pathway consists of a series of signaling events activated in response to diverse stress and physiological conditions such as food deprivation,...
Delivery Pathways to the Lysosome
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
Autophagic Cell Death
Autophagy and Apoptosis
Autophagy can activate apoptosis. In normal conditions, the autophagy activating protein Beclin-1 and...
The Unfolded Protein Response
Export of Misfolded Proteins out of the ER
Regulation of the Unfolded Protein Response

