Literature DB >> 23485338

Blessings in disguise: biological benefits of prion-like mechanisms.

Gregory A Newby1, Susan Lindquist.   

Abstract

Prions and amyloids are often associated with disease, but related mechanisms provide beneficial functions in nature. Prion-like mechanisms (PriLiMs) are found from bacteria to humans, where they alter the biological and physical properties of prion-like proteins. We have proposed that prions can serve as heritable bet-hedging devices for diversifying microbial phenotypes. Other, more dynamic proteinaceous complexes may be governed by similar self-templating conformational switches. Additional PriLiMs continue to be identified and many share features of self-templating protein structure (including amyloids) and dependence on chaperone proteins. Here, we discuss several PriLiMs and their functions, intending to spur discussion and collaboration on the subject of beneficial prion-like behaviors.
Copyright © 2013 Elsevier Ltd. All rights reserved.

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Year:  2013        PMID: 23485338     DOI: 10.1016/j.tcb.2013.01.007

Source DB:  PubMed          Journal:  Trends Cell Biol        ISSN: 0962-8924            Impact factor:   20.808


  74 in total

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2.  A bacterial global regulator forms a prion.

Authors:  Andy H Yuan; Ann Hochschild
Journal:  Science       Date:  2017-01-13       Impact factor: 47.728

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Authors:  Yi Kuang; Marcus J C Long; Jie Zhou; Junfeng Shi; Yuan Gao; Chen Xu; Lizbeth Hedstrom; Bing Xu
Journal:  J Biol Chem       Date:  2014-08-25       Impact factor: 5.157

4.  Functional role of Tia1/Pub1 and Sup35 prion domains: directing protein synthesis machinery to the tubulin cytoskeleton.

Authors:  Xiang Li; Joseph B Rayman; Eric R Kandel; Irina L Derkatch
Journal:  Mol Cell       Date:  2014-06-26       Impact factor: 17.970

5.  Self-assembled FUS binds active chromatin and regulates gene transcription.

Authors:  Liuqing Yang; Jozsef Gal; Jing Chen; Haining Zhu
Journal:  Proc Natl Acad Sci U S A       Date:  2014-12-01       Impact factor: 11.205

Review 6.  Neurodegenerative diseases: expanding the prion concept.

Authors:  Lary C Walker; Mathias Jucker
Journal:  Annu Rev Neurosci       Date:  2015-03-30       Impact factor: 12.449

7.  Engineered protein disaggregases mitigate toxicity of aberrant prion-like fusion proteins underlying sarcoma.

Authors:  Jeremy J Ryan; Macy L Sprunger; Kayla Holthaus; James Shorter; Meredith E Jackrel
Journal:  J Biol Chem       Date:  2019-06-05       Impact factor: 5.157

8.  Potentiating Hsp104 activity via phosphomimetic mutations in the middle domain.

Authors:  Amber Tariq; JiaBei Lin; Megan M Noll; Mariana P Torrente; Korrie L Mack; Oscar Hernandez Murillo; Meredith E Jackrel; James Shorter
Journal:  FEMS Yeast Res       Date:  2018-08-01       Impact factor: 2.796

9.  Potentiated Hsp104 variants antagonize diverse proteotoxic misfolding events.

Authors:  Meredith E Jackrel; Morgan E DeSantis; Bryan A Martinez; Laura M Castellano; Rachel M Stewart; Kim A Caldwell; Guy A Caldwell; James Shorter
Journal:  Cell       Date:  2014-01-16       Impact factor: 41.582

10.  Prion-like proteins sequester and suppress the toxicity of huntingtin exon 1.

Authors:  Can Kayatekin; Kent E S Matlack; William R Hesse; Yinghua Guan; Sohini Chakrabortee; Jenny Russ; Erich E Wanker; Jagesh V Shah; Susan Lindquist
Journal:  Proc Natl Acad Sci U S A       Date:  2014-08-04       Impact factor: 11.205

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