» Articles » PMID: 27229621

A Method to Rapidly Create Protein Aggregates in Living Cells

Overview
Journal Nat Commun
Specialty Biology
Date 2016 May 28
PMID 27229621
Citations 17
Authors
Affiliations
Soon will be listed here.
Abstract

The accumulation of protein aggregates is a common pathological hallmark of many neurodegenerative diseases. However, we do not fully understand how aggregates are formed or the complex network of chaperones, proteasomes and other regulatory factors involved in their clearance. Here, we report a chemically controllable fluorescent protein that enables us to rapidly produce small aggregates inside living cells on the order of seconds, as well as monitor the movement and coalescence of individual aggregates into larger structures. This method can be applied to diverse experimental systems, including live animals, and may prove valuable for understanding cellular responses and diseases associated with protein aggregates.

Citing Articles

Temporal control of acute protein aggregate turnover by UBE3C and NRF1-dependent proteasomal pathways.

Hickey K, Panov A, Whelan E, Schafer T, Mizrak A, Kopito R Proc Natl Acad Sci U S A. 2024; 121(50):e2417390121.

PMID: 39636856 PMC: 11648907. DOI: 10.1073/pnas.2417390121.


Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor.

Acharjee M, Ledden B, Thomas B, He X, Messina T, Giurleo J Sensors (Basel). 2024; 24(1).

PMID: 38202943 PMC: 10781269. DOI: 10.3390/s24010081.


Cis P-tau is a central circulating and placental etiologic driver and therapeutic target of preeclampsia.

Jash S, Banerjee S, Cheng S, Wang B, Qiu C, Kondo A Nat Commun. 2023; 14(1):5414.

PMID: 37669931 PMC: 10480164. DOI: 10.1038/s41467-023-41144-6.


Protein quality control and aggregation in the endoplasmic reticulum: From basic to bedside.

Chen G, Wei T, Ju F, Li H Front Cell Dev Biol. 2023; 11:1156152.

PMID: 37152279 PMC: 10154544. DOI: 10.3389/fcell.2023.1156152.


A spider silk-derived solubility domain inhibits nuclear and cytosolic protein aggregation in human cells.

Schellhaus A, Xu S, Gierisch M, Vornberger J, Johansson J, Dantuma N Commun Biol. 2022; 5(1):505.

PMID: 35618760 PMC: 9135726. DOI: 10.1038/s42003-022-03442-5.


References
1.
Finley D . Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem. 2009; 78:477-513. PMC: 3431160. DOI: 10.1146/annurev.biochem.78.081507.101607. View

2.
Banaszynski L, Chen L, Maynard-Smith L, Ooi A, Wandless T . A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules. Cell. 2006; 126(5):995-1004. PMC: 3290523. DOI: 10.1016/j.cell.2006.07.025. View

3.
Ramdzan Y, Polling S, Chia C, Ng I, Ormsby A, Croft N . Tracking protein aggregation and mislocalization in cells with flow cytometry. Nat Methods. 2012; 9(5):467-70. DOI: 10.1038/nmeth.1930. View

4.
Chu B, Kovary K, Guillaume J, Chen L, Teruel M, Wandless T . The E3 ubiquitin ligase UBE3C enhances proteasome processivity by ubiquitinating partially proteolyzed substrates. J Biol Chem. 2013; 288(48):34575-87. PMC: 3843071. DOI: 10.1074/jbc.M113.499350. View

5.
Johnston J, Ward C, Kopito R . Aggresomes: a cellular response to misfolded proteins. J Cell Biol. 1998; 143(7):1883-98. PMC: 2175217. DOI: 10.1083/jcb.143.7.1883. View