Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly

David S.W. Protter, Bhalchandra S. Rao, Briana Van Treeck, Yuan Lin, Laura Mizoue, Michael K. Rosen, Roy Parker

Research output: Contribution to journalArticle

55 Citations (Scopus)

Abstract

Eukaryotic cells contain large RNA-protein assemblies referred to as RNP granules, whose assembly is promoted by both traditional protein interactions and intrinsically disordered protein domains. Using RNP granules as an example, we provide evidence for an assembly mechanism of large cellular structures wherein specific protein-protein or protein-RNA interactions act together with promiscuous interactions of intrinsically disordered regions (IDRs). This synergistic assembly mechanism illuminates RNP granule assembly and explains why many components of RNP granules, and other large dynamic assemblies, contain IDRs linked to specific protein-protein or protein-RNA interaction modules. We suggest assemblies based on combinations of specific interactions and promiscuous IDRs are common features of eukaryotic cells. Many RNA-binding proteins contain disordered regions. Protter et al. find that these regions interact nonspecifically with other proteins, which can disrupt phase separation in vitro. They also find that promiscuous interactions synergize with specific interactions to promote phase separation and formation of higher-order structures, like RNP granules.

Original languageEnglish (US)
Pages (from-to)1401-1412
Number of pages12
JournalCell Reports
Volume22
Issue number6
DOIs
StatePublished - Feb 6 2018

Fingerprint

Proteins
Eukaryotic Cells
RNA
Phase separation
Intrinsically Disordered Proteins
RNA-Binding Proteins
Cellular Structures

Keywords

  • Dhh1
  • intrinsically disordered
  • P-body
  • phase separation
  • RNP granule

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Protter, D. S. W., Rao, B. S., Van Treeck, B., Lin, Y., Mizoue, L., Rosen, M. K., & Parker, R. (2018). Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly. Cell Reports, 22(6), 1401-1412. https://doi.org/10.1016/j.celrep.2018.01.036

Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly. / Protter, David S.W.; Rao, Bhalchandra S.; Van Treeck, Briana; Lin, Yuan; Mizoue, Laura; Rosen, Michael K.; Parker, Roy.

In: Cell Reports, Vol. 22, No. 6, 06.02.2018, p. 1401-1412.

Research output: Contribution to journalArticle

Protter, DSW, Rao, BS, Van Treeck, B, Lin, Y, Mizoue, L, Rosen, MK & Parker, R 2018, 'Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly', Cell Reports, vol. 22, no. 6, pp. 1401-1412. https://doi.org/10.1016/j.celrep.2018.01.036
Protter, David S.W. ; Rao, Bhalchandra S. ; Van Treeck, Briana ; Lin, Yuan ; Mizoue, Laura ; Rosen, Michael K. ; Parker, Roy. / Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly. In: Cell Reports. 2018 ; Vol. 22, No. 6. pp. 1401-1412.
@article{224e160a1f7840619b74dec16798e9e2,
title = "Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly",
abstract = "Eukaryotic cells contain large RNA-protein assemblies referred to as RNP granules, whose assembly is promoted by both traditional protein interactions and intrinsically disordered protein domains. Using RNP granules as an example, we provide evidence for an assembly mechanism of large cellular structures wherein specific protein-protein or protein-RNA interactions act together with promiscuous interactions of intrinsically disordered regions (IDRs). This synergistic assembly mechanism illuminates RNP granule assembly and explains why many components of RNP granules, and other large dynamic assemblies, contain IDRs linked to specific protein-protein or protein-RNA interaction modules. We suggest assemblies based on combinations of specific interactions and promiscuous IDRs are common features of eukaryotic cells. Many RNA-binding proteins contain disordered regions. Protter et al. find that these regions interact nonspecifically with other proteins, which can disrupt phase separation in vitro. They also find that promiscuous interactions synergize with specific interactions to promote phase separation and formation of higher-order structures, like RNP granules.",
keywords = "Dhh1, intrinsically disordered, P-body, phase separation, RNP granule",
author = "Protter, {David S.W.} and Rao, {Bhalchandra S.} and {Van Treeck}, Briana and Yuan Lin and Laura Mizoue and Rosen, {Michael K.} and Roy Parker",
year = "2018",
month = "2",
day = "6",
doi = "10.1016/j.celrep.2018.01.036",
language = "English (US)",
volume = "22",
pages = "1401--1412",
journal = "Cell Reports",
issn = "2211-1247",
publisher = "Cell Press",
number = "6",

}

TY - JOUR

T1 - Intrinsically Disordered Regions Can Contribute Promiscuous Interactions to RNP Granule Assembly

AU - Protter, David S.W.

AU - Rao, Bhalchandra S.

AU - Van Treeck, Briana

AU - Lin, Yuan

AU - Mizoue, Laura

AU - Rosen, Michael K.

AU - Parker, Roy

PY - 2018/2/6

Y1 - 2018/2/6

N2 - Eukaryotic cells contain large RNA-protein assemblies referred to as RNP granules, whose assembly is promoted by both traditional protein interactions and intrinsically disordered protein domains. Using RNP granules as an example, we provide evidence for an assembly mechanism of large cellular structures wherein specific protein-protein or protein-RNA interactions act together with promiscuous interactions of intrinsically disordered regions (IDRs). This synergistic assembly mechanism illuminates RNP granule assembly and explains why many components of RNP granules, and other large dynamic assemblies, contain IDRs linked to specific protein-protein or protein-RNA interaction modules. We suggest assemblies based on combinations of specific interactions and promiscuous IDRs are common features of eukaryotic cells. Many RNA-binding proteins contain disordered regions. Protter et al. find that these regions interact nonspecifically with other proteins, which can disrupt phase separation in vitro. They also find that promiscuous interactions synergize with specific interactions to promote phase separation and formation of higher-order structures, like RNP granules.

AB - Eukaryotic cells contain large RNA-protein assemblies referred to as RNP granules, whose assembly is promoted by both traditional protein interactions and intrinsically disordered protein domains. Using RNP granules as an example, we provide evidence for an assembly mechanism of large cellular structures wherein specific protein-protein or protein-RNA interactions act together with promiscuous interactions of intrinsically disordered regions (IDRs). This synergistic assembly mechanism illuminates RNP granule assembly and explains why many components of RNP granules, and other large dynamic assemblies, contain IDRs linked to specific protein-protein or protein-RNA interaction modules. We suggest assemblies based on combinations of specific interactions and promiscuous IDRs are common features of eukaryotic cells. Many RNA-binding proteins contain disordered regions. Protter et al. find that these regions interact nonspecifically with other proteins, which can disrupt phase separation in vitro. They also find that promiscuous interactions synergize with specific interactions to promote phase separation and formation of higher-order structures, like RNP granules.

KW - Dhh1

KW - intrinsically disordered

KW - P-body

KW - phase separation

KW - RNP granule

UR - http://www.scopus.com/inward/record.url?scp=85041735745&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85041735745&partnerID=8YFLogxK

U2 - 10.1016/j.celrep.2018.01.036

DO - 10.1016/j.celrep.2018.01.036

M3 - Article

C2 - 29425497

AN - SCOPUS:85041735745

VL - 22

SP - 1401

EP - 1412

JO - Cell Reports

JF - Cell Reports

SN - 2211-1247

IS - 6

ER -