Related Experiment Video
Updated: May 13, 2026

11:31
Metabolic Labeling of Leucine Rich Repeat Kinases 1 and 2 with Radioactive Phosphate
Published on: September 18, 2013
Protein interacting with C kinase and neurological disorders
Marylène C Focant1, Emmanuel Hermans
1Institute of Neuroscience, Université catholique de Louvain, Brussels, Belgium.
Synapse (New York, N.Y.)
|February 26, 2013
Summary
The protein interacting with C kinase (PICK1) is crucial for synaptic function and is implicated in neurological disorders. Research highlights PICK1
Area of Science:
- Neurobiology
- Molecular Neuroscience
- Cell Biology
Background:
- The protein interacting with C kinase (PICK1) is a key regulator of excitatory synapse activity.
- PICK1 contains a PDZ domain and interacts with numerous synaptic proteins, including receptors, transporters, and enzymes.
- Its lipid-binding domain targets PICK1 to the cell membrane, influencing partner localization and function.
Purpose of the Study:
- To review recent experimental findings on PICK1's role in neurological disorders.
- To summarize PICK1's involvement in conditions such as schizophrenia, Parkinson's disease, epilepsy, chronic pain, drug abuse, and ALS.
Main Methods:
- Review of existing experimental observations and literature.
- Analysis of genetic and pharmacological manipulations of PICK1.
- Examination of PICK1's interactions with synaptic partners under physiological and pathological conditions.
Main Results:
- PICK1 interacts with a diverse range of synaptic proteins, including GluA2, neurotransmitter receptors, transporters, and serine racemase.
- PICK1's localization and function are critical for synaptic localization and activity of its interacting partners.
- Altered regulation of PICK1 partners under pathological conditions suggests PICK1's involvement in neurological diseases.
Conclusions:
- PICK1 plays a significant role in the pathophysiology of various neurological disorders.
- Modulating PICK1 offers potential therapeutic strategies for neurological conditions.
- Further research into PICK1 interactions is essential for understanding and treating brain disorders.
Related Concept Videos
Enzyme-linked Receptors
Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Neural Regulation
Digestion begins with a cephalic phase that prepares the digestive system to receive food. When our brain processes visual or olfactory information about food, it triggers impulses in the cranial nerves innervating the salivary glands and stomach to prepare for food.
Cytoskeletal Linker Proteins - Plakins
Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
Phosphorylation
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

