Hypothesis and Theory ARTICLE
Nucleolar Sequestration: Remodeling Nucleoli into Amyloid-bodies
- 1University of Miami, United States
This year marks the 20th anniversary of the discovery that the nucleolus can temporarily immobilize proteins, a process known as nucleolar sequestration. This review reflects on the progress made to understand the physiological roles of nucleolar sequestration and the mechanisms involved in the immobilization of proteins. We discuss how protein immobilization can occur through a clever and highly choreographed amyloidogenic program that converts the nucleolus into a large fibrous organelle with amyloid-like characteristics called the Amyloid body (A-body). We propose a working model of A-body biogenesis that includes a role for low complexity ribosomal intergenic spacer RNA (rIGSRNA) and a discrete peptide sequence, the amyloid-converting motif (ACM), found in many proteins that undergo immobilization. Amyloid-bodies provide a unique model to study the multi-step assembly of a membrane-less compartment and may provide alternative insights into pathological amyloidogenesis involved in neurological disorders.
Keywords: Heat shock (HS), Acidosis, Architectural RNA (arcRNA), Alzeimer’s disease, Cellular dormancy, Physiological amyloidogenesis, Beta - amyloid protein
Received: 20 Jul 2019;
Accepted: 24 Oct 2019.
Copyright: © 2019 Wang, Bokros, Theodoridis and Lee. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Prof. Stephen Lee, University of Miami, Coral Gables, 33146, Florida, United States, email@example.com