Literature DB >> 28864230

There Is an Inclusion for That: Material Properties of Protein Granules Provide a Platform for Building Diverse Cellular Functions.

Daniel Kaganovich1.   

Abstract

Proteins perform a staggering variety of functions in the cell. Traditionally, protein function was thought to be hard-wired into the folded structure and conformational dynamics of each protein molecule. Recent work describes a new mode of protein functionality driven by the collective behavior of many different proteins; most of which lack a defined structure. These proteins form clusters or granules in which unstructured polypeptides interact transiently. Nonspecific multivalent interactions drive the formation of phase-separated structures resembling aggregates. This type of functional aggregate granule can be thought of as a single supermolecular functional entity that derives function from its unique material properties. In this review we examine the emerging idea of protein granules as a new functional and structural unit of cellular organization.
Copyright © 2017 Elsevier Ltd. All rights reserved.

Keywords:  RNA–protein granules; aggregation; amyloid; clustering; liquid–liquid phase separation; phase transition

Mesh:

Substances:

Year:  2017        PMID: 28864230     DOI: 10.1016/j.tibs.2017.08.002

Source DB:  PubMed          Journal:  Trends Biochem Sci        ISSN: 0968-0004            Impact factor:   13.807


  14 in total

Review 1.  Mitochondrial dysfunction in protein conformational disorders.

Authors:  Shlomi Brielle; Daniel Kaganovich
Journal:  J Genet       Date:  2018-07       Impact factor: 1.166

2.  Material properties of phase-separated TFEB condensates regulate the autophagy-lysosome pathway.

Authors:  Zheng Wang; Di Chen; Dongshi Guan; Xiaobo Liang; Jianfeng Xue; Hongyu Zhao; Guangtao Song; Jizhong Lou; Yan He; Hong Zhang
Journal:  J Cell Biol       Date:  2022-03-16       Impact factor: 10.539

3.  Iron-induced NCOA4 condensation regulates ferritin fate and iron homeostasis.

Authors:  Sota Kuno; Hiroaki Fujita; Yu-Ki Tanaka; Yasumitsu Ogra; Kazuhiro Iwai
Journal:  EMBO Rep       Date:  2022-03-23       Impact factor: 9.071

4.  Computational resources for identifying and describing proteins driving liquid-liquid phase separation.

Authors:  Rita Pancsa; Wim Vranken; Bálint Mészáros
Journal:  Brief Bioinform       Date:  2021-09-02       Impact factor: 11.622

5.  Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation.

Authors:  Richard S Marshall; Richard D Vierstra
Journal:  Elife       Date:  2018-04-06       Impact factor: 8.713

Review 6.  Tuning up Transcription Factors for Therapy.

Authors:  Attila Becskei
Journal:  Molecules       Date:  2020-04-20       Impact factor: 4.411

7.  Liquid-liquid phase separation in autophagy.

Authors:  Nobuo N Noda; Zheng Wang; Hong Zhang
Journal:  J Cell Biol       Date:  2020-08-03       Impact factor: 10.539

8.  Tuned polymerization of the transcription factor Yan limits off-DNA sequestration to confer context-specific repression.

Authors:  C Matthew Hope; Jemma L Webber; Sherzod A Tokamov; Ilaria Rebay
Journal:  Elife       Date:  2018-11-09       Impact factor: 8.140

9.  Osmolyte accumulation regulates the SUMOylation and inclusion dynamics of the prionogenic Cyc8-Tup1 transcription corepressor.

Authors:  Cory M Nadel; Timothy D Mackie; Richard G Gardner
Journal:  PLoS Genet       Date:  2019-04-22       Impact factor: 5.917

10.  Stress granules inhibit fatty acid oxidation by modulating mitochondrial permeability.

Authors:  Triana Amen; Daniel Kaganovich
Journal:  Cell Rep       Date:  2021-06-15       Impact factor: 9.423

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