APBA2 - Amyloid-Beta A4 Precursor Protein-Binding Family A member 2 | Elisa - Clia - Antibody - Protein

Background:

APBA2, or Amyloid-Beta A4 Precursor Protein-Binding Family A member 2, is a gene that encodes a protein involved in synaptic function and neuronal signaling. It belongs to a family of proteins that bind to the amyloid precursor protein (APP), which is implicated in Alzheimer's disease pathology. The APBA2 protein interacts with the cytoplasmic domain of APP, playing a role in the regulation of APP processing and the generation of amyloid-beta peptide, a hallmark of Alzheimer's disease. Additionally, APBA2 is involved in intracellular signaling pathways and synaptic plasticity, which are crucial for learning and memory processes. Dysregulation of APBA2 function may contribute to Alzheimer's disease progression, although the exact mechanisms are still not fully understood. Studying APBA2 and its interactions with other proteins involved in Alzheimer's disease may provide insights into the underlying molecular mechanisms and potential therapeutic targets for the disease.

Protein Structure:

• N-terminal Domain: The N-terminal region of APBA2 contains a phosphotyrosine-binding (PTB) domain, which is essential for its interaction with the intracellular domain of APP.
• Central Domain: APBA2 features a series of PDZ domains, which facilitate the binding to other proteins and contribute to its role in synaptic scaffolding.
• C-terminal Domain: The C-terminal region is involved in protein-protein interactions and may contribute to the trafficking and processing of APP.

Classification and Subtypes:

APBA2 is part of the X11 family of proteins, which are characterized by their PTB and PDZ domains. The family includes:

• APBA1 (X11): Involved in synaptic vesicle exocytosis and amyloid precursor protein processing.
• APBA3 (X11L2): Functionally similar to APBA1 and APBA2, with roles in APP processing and synaptic function.

Function and Biological Significance:

• APP Processing: APBA2 binds to the intracellular domain of APP, influencing its processing and the generation of amyloid-beta (Aβ) peptides. This interaction is crucial in the context of Alzheimer's disease, where aberrant processing of APP leads to the accumulation of Aβ plaques.
• Synaptic Function: APBA2 is involved in the organization and function of synaptic structures. It acts as a scaffold protein, stabilizing synaptic components and ensuring proper neurotransmitter release.
• Neuronal Development: APBA2 plays roles in neuronal development and maintenance, contributing to the overall health and functionality of neural networks.

Interactions:

• Amyloid Precursor Protein (APP): APBA2 directly interacts with APP through its PTB domain, regulating its processing and the production of amyloid-beta peptides.
• Other Synaptic Proteins: APBA2 interacts with various synaptic proteins through its PDZ domains, forming complexes that are essential for synaptic vesicle exocytosis and neurotransmitter release.

Clinical Issues:

• Alzheimer's Disease: Given its role in APP processing and amyloid-beta generation, APBA2 is implicated in the pathogenesis of Alzheimer's disease. Dysregulation of APBA2 may lead to increased production of amyloid-beta, contributing to the formation of amyloid plaques that are characteristic of the disease.
• Neurodevelopmental Disorders: Mutations or dysregulation of APBA2 could potentially impact neuronal development and function, leading to neurodevelopmental disorders.

Summary:

APBA2 is a neuronal protein that plays critical roles in the processing of amyloid precursor protein (APP), synaptic function, and neuronal development. It interacts with APP through its PTB domain and with other synaptic proteins via its PDZ domains. APBA2's involvement in APP processing links it to the pathogenesis of Alzheimer's disease, making it a significant protein of interest in neurodegenerative research. Additionally, its role in synaptic scaffolding and neurotransmitter release highlights its importance in maintaining healthy neural networks and proper brain function.