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Serine-Arginine Protein Kinase SRPK2 Modulates the Assembly of the Active Zone Scaffolding Protein CAST1/ERC2.
- Source :
-
Cells [Cells] 2019 Oct 29; Vol. 8 (11). Date of Electronic Publication: 2019 Oct 29. - Publication Year :
- 2019
-
Abstract
- Neurons release neurotransmitters at a specialized region of the presynaptic membrane, the active zone (AZ), where a complex meshwork of proteins organizes the release apparatus. The formation of this proteinaceous cytomatrix at the AZ (CAZ) depends on precise homo- and hetero-oligomerizations of distinct CAZ proteins. The CAZ protein CAST1/ERC2 contains four coiled-coil (CC) domains that interact with other CAZ proteins, but also promote self-assembly, which is an essential step for its integration during AZ formation. The self-assembly and synaptic recruitment of the Drosophila protein Bruchpilot (BRP), a partial homolog of CAST1/ERC2, is modulated by the serine-arginine protein kinase (SRPK79D). Here, we demonstrate that overexpression of the vertebrate SRPK2 regulates the self-assembly of CAST1/ERC2 in HEK293T, SH-SY5Y and HT-22 cells and the CC1 and CC4 domains are involved in this process. Moreover, the isoform SRPK2 forms a complex with CAST1/ERC2 when co-expressed in HEK293T and SH-SY5Y cells. More importantly, SRPK2 is present in brain synaptic fractions and synapses, suggesting that this protein kinase might control the level of self-aggregation of CAST1/ERC2 in synapses, and thereby modulate presynaptic assembly.
- Subjects :
- Adaptor Proteins, Signal Transducing chemistry
Animals
Cells, Cultured
Cytoskeletal Proteins chemistry
Embryo, Mammalian
Female
HEK293 Cells
Humans
Neurons cytology
Protein Serine-Threonine Kinases genetics
Rats
Rats, Sprague-Dawley
Synapses chemistry
Synapses genetics
Adaptor Proteins, Signal Transducing metabolism
Cytoskeletal Proteins metabolism
Neurons metabolism
Protein Multimerization genetics
Protein Serine-Threonine Kinases physiology
Synapses metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2073-4409
- Volume :
- 8
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Cells
- Publication Type :
- Academic Journal
- Accession number :
- 31671734
- Full Text :
- https://doi.org/10.3390/cells8111333