잠시만 기다려 주세요. 로딩중입니다.

Mechanisms of Macromolecular Interactions Mediated by Protein Intrinsic Disorder

Molecules and Cells 2020년 43권 11호 p.899 ~ 908
홍성현, 최상민, 김령현, 고준석,
소속 상세정보
홍성현 ( Hong Sung-Hyun ) - Seoul National University School of Biological Sciences
최상민 ( Choi Sang-Min ) - Seoul National University School of Biological Sciences
김령현 ( Kim Ryeong-Hyeon ) - Seoul National University School of Biological Sciences
고준석 ( Koh Jun-Seock ) - Seoul National University School of Biological Sciences

Abstract


Intrinsically disordered proteins or regions (IDPs or IDRs) are widespread in the eukaryotic proteome. Although lacking stable three-dimensional structures in the free forms, IDRs perform critical functions in various cellular processes. Accordingly, mutations and altered expression of IDRs are associated with many pathological conditions. Hence, it is of great importance to understand at the molecular level how IDRs interact with their binding partners. In particular, discovering the unique interaction features of IDRs originating from their dynamic nature may reveal uncharted regulatory mechanisms of specific biological processes. Here we discuss the mechanisms of the macromolecular interactions mediated by IDRs and present the relevant cellular processes including transcription, cell cycle progression, signaling, and nucleocytoplasmic transport. Of special interest is the multivalent binding nature of IDRs driving assembly of multicomponent macromolecular complexes. Integrating the previous theoretical and experimental investigations, we suggest that such IDR-driven multiprotein complexes can function as versatile allosteric switches to process diverse cellular signals. Finally, we discuss the future challenges and potential medical applications of the IDR research.

키워드

allostery; coupled folding and binding; dynamic binding; intrinsically disordered proteins or regions; macromolecular complex; multivalent binding

원문 및 링크아웃 정보

등재저널 정보