Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments
Vasiliy O. Sysoev, Masato Kato, Lillian B. Sutherland, Rong Hu, Steven L. McKnight, Dylan T. Murray
Abstract
Significance The main point of our manuscript is focused on the structure of the low-complexity (LC) domain of the Tm1-I/C intermediate filament protein in the context of assembled intermediate filaments. We found that the LC tail domain of Tm1-I/C exists in precisely the same cross-β conformation within its proper biologic assembly as it does in labile, amyloid-like polymers made from the tail domain alone. This science represents a conceptually distinct advance that may form the cornerstone understanding of how the thousands of LC domains expressed in eukaryotic cells operate in a mechanistic sense, and stands in conflict with previous research claiming that LC domains function in the absence of molecular structure.