Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins

Version 1 : Received: 24 April 2024 / Approved: 24 April 2024 / Online: 24 April 2024 (15:35:56 CEST)

How to cite: Venati, S.R.; Uversky, V.N. Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins. Preprints 2024, 2024041628. https://doi.org/10.20944/preprints202404.1628.v1 Venati, S.R.; Uversky, V.N. Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins. Preprints 2024, 2024041628. https://doi.org/10.20944/preprints202404.1628.v1

Abstract

In this work, we explore the intrinsic disorder status of the three members of the synuclein family of proteins - α-, β-, and γ-synucleins. We also analyzed the peculiarities of the amino acid sequences and modeled 3D structures of the human synuclein family members to find potential effects of pathological mutations. Furthermore, we conducted a comparative sequence-based analysis of the synuclein proteins from various evolutionary distant species and evaluated their levels of intrinsic disorder using a set of commonly used bioinformatics tools. Next, we conducted a detailed functional disorder analysis of the proteins in the interactomes of the human synuclein family members using various web-based disorder analysis and prediction tools, such as RIDAO, D2P2 and FuzDrop. We identify that the interactome of human α-synuclein has relatively higher levels of intrinsic disorder, as compared to the interactomes of human β- and γ- synucleins. These observations highlight the critical importance of intrinsic disorder of human α-synuclein and its interactors in neuronal processes as compared to other proteins of the synuclein family.

Keywords

α-synuclein; β-synuclein; γ-synuclein; intrinsically disordered protein; liquid-liquid phase separation; Parkinson’s disease; protein-protein interactions

Subject

Biology and Life Sciences, Life Sciences

Comments (0)

We encourage comments and feedback from a broad range of readers. See criteria for comments and our Diversity statement.

Leave a public comment
Send a private comment to the author(s)
* All users must log in before leaving a comment
Views 0
Downloads 0
Comments 0
Metrics 0


×
Alerts
Notify me about updates to this article or when a peer-reviewed version is published.
We use cookies on our website to ensure you get the best experience.
Read more about our cookies here.