Analysis of how structural properties of the proteoglycan NG2/CSPG4 relate to its functional traits

What is it about?

The NG2/CSPG4 gene encodes a transmembrane proteoglycan (PG) representing the largest and most structurally complex cell surface-associated molecule of the human proteome. The NG2/CSPG4 transcript shows remarkable evolutionary conservation and, due to the extensive intracellular processing of the translated protein, it generates an array of glycoforms with the potential to execute a wide spectrum of variant-specific molecular interactions. These molecular events are articulated throughout the coaxing of more than 40 ligand molecules and are concurrently operated by the ectodomain and the cytoplasmic tail, whose phosphorylation is tightly controlled by cross-talking signaling pathways. Owing to the multitude of molecular interplays that the PG engages, NG2/CSPG4 stand out for its unique capability to influence virtually all cellular phenomena, spanning from those critically involved in the early phases of embryonic development to those purporting pathological conditions. We discuss here the progresses made in advancing our understanding about the structural-functional bases for the unparalleled ability of NG2/CSPG4 to widely impact on cell behaviour and how its multivalency may be exploited to interfere with disease progression.

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Photo by Hal Gatewood on Unsplash

Photo by Hal Gatewood on Unsplash

Why is it important?

The review article discusses aspects of the multifunctionality of NG2/CSPG4 which have not been dwelled upon in earlier essays. In particular it highlights how the different domains of the macromolecule may engagé different types of molecular interactions with a myriad of ligands, and how these interactions how crucial for cellular functions.

Perspectives