Agglomeration: when folded proteins clump together

• Published in: Biophysical reviews Vol. 15; no. 6; pp. 1987 - 2003
• Main Authors: Romero-Romero, M. L., Garcia-Seisdedos, H.
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer Berlin Heidelberg 01.12.2023; Springer Nature B.V
• Subjects: Agglomeration; Biochemistry; Biological and Medical Physics; Biological Techniques; Biomedical and Life Sciences; Biophysics; Cell Biology; Cellular structure; Life Sciences; Liquid phases; Membrane Biology; Nanotechnology; Phase separation; Proteins; Review; Reviews; Self-assembly; Self-association; Protein assembly; Protein aggregation; Supramolecular assemblies; Biomolecular condensates; Protein-protein interactions
• ISSN: 1867-2450; 1867-2469
• DOI: 10.1007/s12551-023-01172-4

Protein self-association is a widespread phenomenon that results in the formation of multimeric protein structures with critical roles in cellular processes. Protein self-association can lead to finite protein complexes or open-ended, and potentially, infinite structures. This review explores the concept of protein agglomeration, a process that results from the infinite self-assembly of folded proteins. We highlight its differences from other better-described processes with similar macroscopic features, such as aggregation and liquid-liquid phase separation. We review the sequence, structural, and biophysical factors influencing protein agglomeration. Lastly, we briefly discuss the implications of agglomeration in evolution, disease, and aging. Overall, this review highlights the need to study protein agglomeration for a better understanding of cellular processes.