Liprin-α family proteins and their cellular functions.

The spatial organization of subcellular compartments relies on scaffold proteins that facilitate interactions with specific binding partners. Prior research has shown scaffold proteins are essential for assembling cellular structures and regulating signaling pathways. However, the full range of functions for the liprin-α family remains unclear. It was already known that these proteins are involved in synaptic and non-synaptic processes. Yet, the extent of their roles in both neuronal and non-neuronal cells has not been fully characterized. This gap motivated a review of liprin-α's contributions to cellular organization. No prior work had resolved how liprin-α's interactions influence membrane-less compartment formation. This uncertainty drove the need to synthesize current knowledge on liprin-α's roles and mechanisms.

This review aimed to clarify the cellular roles of liprin-α proteins by summarizing their interactions and signaling pathways. The specific problem addressed is the lack of comprehensive understanding of how liprin-α contributes to synaptic and non-synaptic functions. The motivation stems from the proteins' widespread expression and involvement in multiple cellular processes. The study sought to identify which mechanisms govern liprin-α's function in presynaptic and postsynaptic contexts. It also aimed to explore how these proteins regulate cell adhesion and motility. The authors propose that liprin-α's role in phase separation is a key area needing further exploration. This review focuses on synthesizing evidence to highlight liprin-α's importance in cellular organization. The goal is to provide a structured overview of current findings and regulatory mechanisms.

The authors conducted a literature review to compile findings on liprin-α's cellular functions. They analyzed interactions between liprin-α and binding partners across multiple cell types. The approach included examining presynaptic and postsynaptic roles in neurons and non-neuronal cells. The study also evaluated liprin-α's involvement in cell adhesion and motility. The authors focused on signaling pathways associated with liprin-α's functions. They examined evidence for phase separation as a regulatory mechanism. The review approach included comparing findings from diverse experimental models. This synthesis highlights key findings from the literature on liprin-α's roles and mechanisms.

Liprin-α proteins contribute to presynaptic active zone formation and neurotransmitter release. They promote synaptic vesicle accumulation in presynaptic terminals. Evidence suggests liprin-α influences dendritic growth and spinogenesis in postsynaptic regions. AMPA receptor trafficking is also associated with liprin-α activity. Liprin-α1 regulates cell adhesion and motility in non-neuronal cells. The proteins undergo multivalent interactions and liquid-liquid phase separation. This mechanism is proposed to facilitate membrane-less compartment formation. These findings highlight liprin-α's roles in both synaptic and non-synaptic contexts.

The authors synthesize evidence that liprin-α proteins are involved in multiple cellular functions. Their findings suggest these proteins regulate synaptic and non-synaptic processes. The review emphasizes liprin-α's interactions and signaling pathways in presynaptic and postsynaptic contexts. The authors propose that phase separation is a key regulatory mechanism for liprin-α. They suggest this mechanism may promote membrane-less compartment formation. The review highlights liprin-α's role in cell adhesion and motility. The authors conclude that liprin-α's functions are widespread due to its ubiquitous expression. These findings imply that liprin-α is a central player in cellular organization.