Interaction kinetics reveal distinct properties of
conformational ensembles of three-repeat and four-repeat tau
proteins

J 2022

Interaction kinetics reveal distinct properties of conformational ensembles of three-repeat and four-repeat tau proteins

HORNAKOVA, Lenka, Jakub SINSKY, Maria JANUBOVA, Anna MEDERLYOVA, Natalia Paulenka IVANOVOVA et. al.

Základní údaje

Originální název

Interaction kinetics reveal distinct properties of conformational ensembles of three-repeat and four-repeat tau proteins

Autoři

HORNAKOVA, Lenka, Jakub SINSKY, Maria JANUBOVA, Anna MEDERLYOVA, Natalia Paulenka IVANOVOVA, Juraj PIESTANSKY, Andrej KOVAC, Jaroslav GALBA, Rostislav SKRABANA a Ondrej CEHLAR

Vydání

FEBS Letters, Hoboken, Wiley, 2022, 0014-5793

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.500

Kód RIV

RIV/00216224:14740/22:00128730

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1002/1873-3468.14339

UT WoS

000774661700001

Klíčová slova anglicky

aggregation; conformational ensemble; crosslinking mass spectrometry; intrinsically disordered proteins; microscale thermophoresis; surface plasmon resonance

Štítky

CF BIC, ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 27. 2. 2023 20:18, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Tau protein is an intrinsically disordered protein. Its physiological state is best described as a conformational ensemble (CE) of metastable structures interconverting on the local and molecular scale. The monoclonal antibody DC39C recognizes a linear C-terminal tau epitope, and as the tau interaction partner, its binding parameters report about tau CE. Association kinetics of DC39C binding, together with crosslinking mass spectrometry, show differences in the accessibility of the C terminus in CEs of tau isoforms. Furthermore, removal of the C terminus accelerated the aggregation kinetics of three-repeat tau proteins. Our results suggest a novel mechanism of splicing-driven regulation of the tau C-terminal domain with consequences on the specific roles of tau isoforms in microtubule assembly and pathological aggregation. Keywords

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

HORNAKOVA, Lenka, Jakub SINSKY, Maria JANUBOVA, Anna MEDERLYOVA, Natalia Paulenka IVANOVOVA, Juraj PIESTANSKY, Andrej KOVAC, Jaroslav GALBA, Rostislav SKRABANA a Ondrej CEHLAR. Interaction kinetics reveal distinct properties of conformational ensembles of three-repeat and four-repeat tau proteins. FEBS Letters. Hoboken: Wiley, 2022, roč. 596, č. 9, s. 1178-1189. ISSN 0014-5793. Dostupné z: https://dx.doi.org/10.1002/1873-3468.14339.

@article{2262017,
   author = {Hornakova, Lenka and Sinsky, Jakub and Janubova, Maria and Mederlyova, Anna and Ivanovova, Natalia Paulenka and Piestansky, Juraj and Kovac, Andrej and Galba, Jaroslav and Skrabana, Rostislav and Cehlar, Ondrej},
   article_location = {Hoboken},
   article_number = {9},
   doi = {http://dx.doi.org/10.1002/1873-3468.14339},
   keywords = {aggregation; conformational ensemble; crosslinking mass spectrometry; intrinsically disordered proteins; microscale thermophoresis; surface plasmon resonance},
   language = {eng},
   issn = {0014-5793},
   journal = {FEBS Letters},
   title = {Interaction kinetics reveal distinct properties of conformational ensembles of three-repeat and four-repeat tau proteins},
   url = {https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14339},
   volume = {596},
   year = {2022}
}

TY  - JOUR
ID  - 2262017
AU  - Hornakova, Lenka - Sinsky, Jakub - Janubova, Maria - Mederlyova, Anna - Ivanovova, Natalia Paulenka - Piestansky, Juraj - Kovac, Andrej - Galba, Jaroslav - Skrabana, Rostislav - Cehlar, Ondrej
PY  - 2022
TI  - Interaction kinetics reveal distinct properties of conformational ensembles of three-repeat and four-repeat tau proteins
JF  - FEBS Letters
VL  - 596
IS  - 9
SP  - 1178-1189
EP  - 1178-1189
PB  - Wiley
SN  - 00145793
KW  - aggregation
KW  - conformational ensemble
KW  - crosslinking mass spectrometry
KW  - intrinsically disordered proteins
KW  - microscale thermophoresis
KW  - surface plasmon resonance
UR  - https://febs.onlinelibrary.wiley.com/doi/10.1002/1873-3468.14339
N2  - Tau protein is an intrinsically disordered protein. Its physiological state is best described as a conformational ensemble (CE) of metastable structures interconverting on the local and molecular scale. The monoclonal antibody DC39C recognizes a linear C-terminal tau epitope, and as the tau interaction partner, its binding parameters report about tau CE. Association kinetics of DC39C binding, together with crosslinking mass spectrometry, show differences in the accessibility of the C terminus in CEs of tau isoforms. Furthermore, removal of the C terminus accelerated the aggregation kinetics of three-repeat tau proteins. Our results suggest a novel mechanism of splicing-driven regulation of the tau C-terminal domain with consequences on the specific roles of tau isoforms in microtubule assembly and pathological aggregation. Keywords
ER  -

HORNAKOVA, Lenka, Jakub SINSKY, Maria JANUBOVA, Anna MEDERLYOVA, Natalia Paulenka IVANOVOVA, Juraj PIESTANSKY, Andrej KOVAC, Jaroslav GALBA, Rostislav SKRABANA a Ondrej CEHLAR. Interaction kinetics reveal distinct properties of conformational ensembles of three-repeat and four-repeat tau proteins. \textit{FEBS Letters}. Hoboken: Wiley, 2022, roč.~596, č.~9, s.~1178-1189. ISSN~0014-5793. Dostupné z: https://dx.doi.org/10.1002/1873-3468.14339.

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