A working model for condensate RNA-binding proteins as matchmakers for protein complex assembly Journal Article


Authors: Chen, X.; Mayr, C.
Article Title: A working model for condensate RNA-binding proteins as matchmakers for protein complex assembly
Abstract: Most cellular processes are carried out by protein complexes, but it is still largely unknown how the subunits of lowly expressed complexes find each other in the crowded cellular environment. Here, we will describe a working model where RNA-binding proteins in cytoplasmic condensates act as matchmakers between their bound proteins (called protein targets) and newly translated proteins of their RNA targets to promote their assembly into complexes. Different RNA-binding proteins act as scaffolds for various cytoplasmic condensates with several of them supporting translation. mRNAs and proteins are recruited into the cytoplasmic condensates through binding to specific domains in the RNA-binding proteins. Scaffold RNA-binding proteins have a high valency. In our model, they use homotypic interactions to assemble condensates and they use heterotypic interactions to recruit protein targets into the condensates. We propose that unoccupied binding sites in the scaffold RNA-binding proteins transiently retain recruited and newly translated proteins in the condensates, thus promoting their assembly into complexes. Taken together, we propose that lowly expressed subunits of protein complexes combine information in their mRNAs and proteins to colocalize in the cytoplasm. The efficiency of protein complex assembly is increased by transient entrapment accomplished by multivalent RNA-binding proteins within cytoplasmic condensates. © 2022 Cold Spring Harbor Laboratory Press. All rights reserved.
Keywords: cooperativity between mrna and protein motifs; cytoplasmic compartmentalization: subcellular organization; function of biomolecular condensates; localized processes; protein–protein interaction
Journal Title: RNA
Volume: 28
Issue: 1
ISSN: 1355-8382
Publisher: Cold Spring Harbor Laboratory Press  
Date Published: 2022-01-01
Start Page: 76
End Page: 87
Language: English
DOI: 10.1261/rna.078995.121
PUBMED: 34706978
PROVIDER: scopus
PMCID: PMC8675283
DOI/URL:
Notes: Article -- Export Date: 3 January 2022 -- Source: Scopus
Altmetric
Citation Impact
MSK Authors
  1. Christine Mayr
    23 Mayr
  2. Xiuzhen Chen
    1 Chen