English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Protein disorder, prion propensities, and self-organizing macromolecular collectives.

Malinovska, L., Kroschwald, S., & Alberti, S. (2013). Protein disorder, prion propensities, and self-organizing macromolecular collectives. Biochimica et Biophysica Acta, 1834(5), 918-931.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Malinovska, Liliana1, Author           
Kroschwald, Sonja1, Author           
Alberti, Simon1, Author           
Affiliations:
1Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society, ou_2340692              

Content

show
hide
Free keywords: -
 Abstract: Eukaryotic cells are partitioned into functionally distinct self-organizing compartments. But while the biogenesis of membrane-surrounded compartments is beginning to be understood, the organizing principles behind large membrane-less structures, such as RNA-containing granules, remain a mystery. Here, we argue that protein disorder is an essential ingredient for the formation of such macromolecular collectives. Intrinsically disordered regions (IDRs) do not fold into a well-defined structure but rather sample a range of conformational states, depending on the local conditions. In addition to being structurally versatile, IDRs promote multivalent and transient interactions. This unique combination of features turns intrinsically disordered proteins into ideal agents to orchestrate the formation of large macromolecular assemblies. The presence of conformationally flexible regions, however, comes at a cost, for many intrinsically disordered proteins are aggregation-prone and cause protein misfolding diseases. This association with disease is particularly strong for IDRs with prion-like amino acid composition. Here, we examine how disease-causing and normal conformations are linked, and discuss the possibility that the dynamic order of the cytoplasm emerges, at least in part, from the collective properties of intrinsically disordered prion-like domains. This article is part of a Special Issue entitled: The emerging dynamic view of proteins: Protein plasticity in allostery, evolution and self-assembly.

Details

show
hide
Language(s):
 Dates: 2013
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 688509
Other: 5104
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochimica et Biophysica Acta
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 1834 (5) Sequence Number: - Start / End Page: 918 - 931 Identifier: -