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There Is an inclusion for that: material properties of protein granules provide a platform for building diverse cellular functions

There Is an inclusion for that: material properties of protein granules provide a platform for building diverse cellular functions
There Is an inclusion for that: material properties of protein granules provide a platform for building diverse cellular functions
Review: 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.
Cell Physiological Phenomena, Humans, Proteins/chemistry
0968-0004
765-776
Kaganovich, Daniel
ebb13f4e-e925-4aef-88e7-ddc25ef52d8f
Kaganovich, Daniel
ebb13f4e-e925-4aef-88e7-ddc25ef52d8f

Kaganovich, Daniel (2017) There Is an inclusion for that: material properties of protein granules provide a platform for building diverse cellular functions. Trends in Biochemical Sciences, 42 (10), 765-776. (doi:10.1016/j.tibs.2017.08.002).

Record type: Review

Abstract

Review: 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.

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More information

e-pub ahead of print date: 29 August 2017
Published date: 1 October 2017
Additional Information: Copyright © 2017 Elsevier Ltd. All rights reserved.
Keywords: Cell Physiological Phenomena, Humans, Proteins/chemistry

Identifiers

Local EPrints ID: 475598
URI: http://eprints.soton.ac.uk/id/eprint/475598
ISSN: 0968-0004
PURE UUID: 6c65ffe1-dfcf-428e-9ffa-cb2eb960564d
ORCID for Daniel Kaganovich: ORCID iD orcid.org/0000-0003-2398-1596

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Date deposited: 22 Mar 2023 17:34
Last modified: 17 Mar 2024 04:17

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Author: Daniel Kaganovich ORCID iD

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