Liquid-Liquid Phase Separation Primes Spider Silk Proteins for Fiber Formation via a Conditional Sticker Domain

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Standard

Liquid-Liquid Phase Separation Primes Spider Silk Proteins for Fiber Formation via a Conditional Sticker Domain. / Leppert, Axel; Chen, Gefei; Lama, Dilraj; Sahin, Cagla; Railaite, Vaida; Shilkova, Olga; Arndt, Tina; Marklund, Erik G.; Lane, David P.; Rising, Anna; Landreh, Michael.

I: Nano Letters, Bind 23, Nr. 12, 2023.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Leppert, A, Chen, G, Lama, D, Sahin, C, Railaite, V, Shilkova, O, Arndt, T, Marklund, EG, Lane, DP, Rising, A & Landreh, M 2023, 'Liquid-Liquid Phase Separation Primes Spider Silk Proteins for Fiber Formation via a Conditional Sticker Domain', Nano Letters, bind 23, nr. 12. https://doi.org/10.1021/acs.nanolett.3c00773

APA

Leppert, A., Chen, G., Lama, D., Sahin, C., Railaite, V., Shilkova, O., Arndt, T., Marklund, E. G., Lane, D. P., Rising, A., & Landreh, M. (2023). Liquid-Liquid Phase Separation Primes Spider Silk Proteins for Fiber Formation via a Conditional Sticker Domain. Nano Letters, 23(12). https://doi.org/10.1021/acs.nanolett.3c00773

Vancouver

Leppert A, Chen G, Lama D, Sahin C, Railaite V, Shilkova O o.a. Liquid-Liquid Phase Separation Primes Spider Silk Proteins for Fiber Formation via a Conditional Sticker Domain. Nano Letters. 2023;23(12). https://doi.org/10.1021/acs.nanolett.3c00773

Author

Leppert, Axel ; Chen, Gefei ; Lama, Dilraj ; Sahin, Cagla ; Railaite, Vaida ; Shilkova, Olga ; Arndt, Tina ; Marklund, Erik G. ; Lane, David P. ; Rising, Anna ; Landreh, Michael. / Liquid-Liquid Phase Separation Primes Spider Silk Proteins for Fiber Formation via a Conditional Sticker Domain. I: Nano Letters. 2023 ; Bind 23, Nr. 12.

Bibtex

@article{eec597f51991475292ac651611fb69f7,
title = "Liquid-Liquid Phase Separation Primes Spider Silk Proteins for Fiber Formation via a Conditional Sticker Domain",
abstract = "Many protein condensates can convert to fibrillar aggregates, but the underlying mechanisms are unclear. Liquid-liquid phase separation (LLPS) of spider silk proteins, spidroins, suggests a regulatory switch between both states. Here, we combine microscopy and native mass spectrometry to investigate the influence of protein sequence, ions, and regulatory domains on spidroin LLPS. We find that salting out-effects drive LLPS via low-affinity stickers in the repeat domains. Interestingly, conditions that enable LLPS simultaneously cause dissociation of the dimeric C-terminal domain (CTD), priming it for aggregation. Since the CTD enhances LLPS of spidroins but is also required for their conversion into amyloid-like fibers, we expand the stickers and spacers-model of phase separation with the concept of folded domains as conditional stickers that represent regulatory units.",
keywords = "functional amyloid, native mass spectrometry, Phase separation, stickers and spacers-model",
author = "Axel Leppert and Gefei Chen and Dilraj Lama and Cagla Sahin and Vaida Railaite and Olga Shilkova and Tina Arndt and Marklund, {Erik G.} and Lane, {David P.} and Anna Rising and Michael Landreh",
note = "Publisher Copyright: {\textcopyright} 2023 The Authors. Published by American Chemical Society.",
year = "2023",
doi = "10.1021/acs.nanolett.3c00773",
language = "English",
volume = "23",
journal = "Nano Letters",
issn = "1530-6984",
publisher = "American Chemical Society",
number = "12",

}

RIS

TY - JOUR

T1 - Liquid-Liquid Phase Separation Primes Spider Silk Proteins for Fiber Formation via a Conditional Sticker Domain

AU - Leppert, Axel

AU - Chen, Gefei

AU - Lama, Dilraj

AU - Sahin, Cagla

AU - Railaite, Vaida

AU - Shilkova, Olga

AU - Arndt, Tina

AU - Marklund, Erik G.

AU - Lane, David P.

AU - Rising, Anna

AU - Landreh, Michael

N1 - Publisher Copyright: © 2023 The Authors. Published by American Chemical Society.

PY - 2023

Y1 - 2023

N2 - Many protein condensates can convert to fibrillar aggregates, but the underlying mechanisms are unclear. Liquid-liquid phase separation (LLPS) of spider silk proteins, spidroins, suggests a regulatory switch between both states. Here, we combine microscopy and native mass spectrometry to investigate the influence of protein sequence, ions, and regulatory domains on spidroin LLPS. We find that salting out-effects drive LLPS via low-affinity stickers in the repeat domains. Interestingly, conditions that enable LLPS simultaneously cause dissociation of the dimeric C-terminal domain (CTD), priming it for aggregation. Since the CTD enhances LLPS of spidroins but is also required for their conversion into amyloid-like fibers, we expand the stickers and spacers-model of phase separation with the concept of folded domains as conditional stickers that represent regulatory units.

AB - Many protein condensates can convert to fibrillar aggregates, but the underlying mechanisms are unclear. Liquid-liquid phase separation (LLPS) of spider silk proteins, spidroins, suggests a regulatory switch between both states. Here, we combine microscopy and native mass spectrometry to investigate the influence of protein sequence, ions, and regulatory domains on spidroin LLPS. We find that salting out-effects drive LLPS via low-affinity stickers in the repeat domains. Interestingly, conditions that enable LLPS simultaneously cause dissociation of the dimeric C-terminal domain (CTD), priming it for aggregation. Since the CTD enhances LLPS of spidroins but is also required for their conversion into amyloid-like fibers, we expand the stickers and spacers-model of phase separation with the concept of folded domains as conditional stickers that represent regulatory units.

KW - functional amyloid

KW - native mass spectrometry

KW - Phase separation

KW - stickers and spacers-model

U2 - 10.1021/acs.nanolett.3c00773

DO - 10.1021/acs.nanolett.3c00773

M3 - Journal article

C2 - 37084706

AN - SCOPUS:85154035880

VL - 23

JO - Nano Letters

JF - Nano Letters

SN - 1530-6984

IS - 12

ER -

ID: 346048164