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- W1994131467 abstract "IDPs (intrinsically disordered proteins) are highly abundant in eukaryotic proteomes and important for cellular functions, especially in cell signalling and transcriptional regulation. An IDR (intrinsically disordered region) within an IDP often undergoes disorder-to-order transitions upon binding to various partners, allowing an IDP to recognize and bind different partners at various binding interfaces. Plant-specific GRAS proteins play critical and diverse roles in plant development and signalling, and act as integrators of signals from multiple plant growth regulatory and environmental inputs. Possessing an intrinsically disordered N-terminal domain, the GRAS proteins constitute the first functionally required unfoldome from the plant kingdom. Furthermore, the N-terminal domains of GRAS proteins contain MoRFs (molecular recognition features), short interaction-prone segments that are located within IDRs and are able to recognize their interacting partners by undergoing disorder-to-order transitions upon binding to these specific partners. These MoRFs represent potential protein–protein binding sites and may be acting as molecular bait in recognition events during plant development. Intrinsic disorder provides GRAS proteins with a degree of binding plasticity that may be linked to their functional versatility. As an overview of structure–function relationships for GRAS proteins, the present review covers the main biological functions of the GRAS family, the IDRs within these proteins and their implications for understanding mode-of-action." @default.
- W1994131467 created "2016-06-24" @default.
- W1994131467 creator A5046702073 @default.
- W1994131467 creator A5068425729 @default.
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- W1994131467 date "2012-01-27" @default.
- W1994131467 modified "2023-10-01" @default.
- W1994131467 title "GRAS proteins: the versatile roles of intrinsically disordered proteins in plant signalling" @default.
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- W1994131467 doi "https://doi.org/10.1042/bj20111766" @default.
- W1994131467 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22280012" @default.
- W1994131467 hasPublicationYear "2012" @default.
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