Related Experiment Video
Updated: Mar 24, 2026
11:11
Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
Published on: February 21, 2019
7.9K
Multiple faces of protein interacting with C kinase 1 (PICK1): Structure, function, and diseases
Yun-Hong Li1, Nan Zhang1, Ya-Nan Wang2
1Key Laboratory of Craniocerebral Diseases of Ningxia Hui Autonomous Region, Ningxia Medical University, Yinchuan, Ningxia 750004, China.
Neurochemistry International
|March 13, 2016
Summary
Protein Interacting with C-kinase 1 (PICK1) is a unique protein regulating membrane protein trafficking. This review explores PICK1
Area of Science:
- Molecular and Cellular Biology
- Neuroscience
- Biochemistry
Background:
- Protein Interacting with C-kinase 1 (PICK1) possesses both PDZ and BAR domains, enabling interaction with numerous membrane proteins and lipids.
- PICK1 is widely expressed, with high abundance in the brain and testis, indicating diverse functional roles.
Purpose of the Study:
- To review recent advances in the structure, regulation, and functions of PICK1.
- To summarize PICK1's role in protein trafficking and its involvement in various diseases.
Main Methods:
- Literature review of studies on PICK1 structure, function, and disease association.
- Analysis of PICK1's interactions with neurotransmitter receptors, transporters, and ion channels.
- Examination of PICK1's role in neurological and non-neurological disease pathogenesis.
Main Results:
- PICK1 regulates the trafficking of AMPA receptor subunit GluA2 during synaptic plasticity (LTD and LTP).
- PICK1 is implicated in diverse neurological disorders including chronic pain, epilepsy, stroke, and Parkinson's disease.
- PICK1 also plays a role in non-neurological conditions such as globozoospermia, breast cancer, and heart failure.
Conclusions:
- PICK1 is a multifunctional protein critical for protein trafficking and cellular regulation.
- Dysregulation of PICK1 is associated with a wide spectrum of human diseases, highlighting its therapeutic potential.
More Related Videos
Related Concept Videos
02:54Protein Kinases and Phosphatases
15.5K
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...
15.5K
02:54Protein Kinases and Phosphatases
4.7K
4.7K
01:20The JAK-STAT Signaling Pathway
13.8K
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
13.8K
01:30Assembly of Signaling Complexes
7.1K
Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
7.1K
02:04Protein-protein Interfaces
15.0K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
15.0K
01:19Interactions Between Signaling Pathways
7.9K
Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...
7.9K