Recombinant VILIP1 Protein Standard (His tag)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Visinin-like protein 1 commonly abbreviated as VILIP1 is a neuronal calcium sensor protein. It has a mass of about 22 kDa and consists of four EF-hand motifs that bind calcium ions. VILIP1 is primarily expressed in the central nervous system including regions such as the hippocampus and cerebral cortex. This protein interacts with membranes and other intracellular molecular targets in response to changes in calcium levels influencing cellular activities associated with calcium signaling.

Biological function summary

Visinin-like protein 1 modulates various physiological processes within neurons. It regulates signal transduction pathways by mediating calcium-dependent interactions with other proteins. VILIP1 may be part of complexes with other signaling proteins that participate in neurotransmitter release and synaptic plasticity. Its ability to modulate the phosphorylation status of its binding partners can influence neuronal excitability and synaptic communication.

Pathways

Various studies highlight how visinin-like protein 1 participates in critical signaling modules. This protein contributes to the regulation of the cAMP signaling pathway where it can affect the activation of adenylate cyclase. Moreover VILIP1 interacts with signaling pathways related to nicotinic acetylcholine receptors affecting the transmission of nerve impulses. It influences the dynamics between calcium signaling and cAMP affecting processes like learning and memory.

Visinin-like protein 1 relates significantly to neurodegenerative diseases. Research findings associate elevated VILIP1 levels with Alzheimer's disease where it can serve as a biomarker for disease progression. Furthermore it connects to Parkinson's disease given its role in neuronal calcium homeostasis a critical factor in disease pathology. In Alzheimer's disease VILIP1 levels can correlate with beta-amyloid plaque development and tau protein phosphorylation.