The Hydrophilic Loop of Arabidopsis PIN1 Auxin Efflux Carrier
Harbors Hallmarks of an Intrinsically Disordered Protein

J 2022

The Hydrophilic Loop of Arabidopsis PIN1 Auxin Efflux Carrier Harbors Hallmarks of an Intrinsically Disordered Protein

BILANOVIČOVÁ, Veronika, Nikola RÝDZA, Lilla KOCZKA, Martin HESS, Elena FERARU et. al.

Základní údaje

Originální název

The Hydrophilic Loop of Arabidopsis PIN1 Auxin Efflux Carrier Harbors Hallmarks of an Intrinsically Disordered Protein

Autoři

BILANOVIČOVÁ, Veronika (703 Slovensko, domácí), Nikola RÝDZA (703 Slovensko, domácí), Lilla KOCZKA (348 Maďarsko, domácí), Martin HESS (203 Česká republika, domácí), Elena FERARU, Jiri FRIML a Tomasz NODZYNSKI (616 Polsko, garant, domácí)

Vydání

International Journal of Molecular Sciences, Basel, Multidisciplinary Digital Publishing Institute, 2022, 1422-0067

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Švýcarsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 5.600

Kód RIV

RIV/00216224:14740/22:00128182

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.3390/ijms23116352

UT WoS

000808733300001

Klíčová slova anglicky

PIN1; hydrophilic hoop; dimerization; intrinsic disorder; subcellular trafficking

Štítky

CF BIC, CF CELLIM, CF PLANT, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 15. 10. 2024 14:10, Ing. Marie Švancarová

Anotace

V originále

Much of plant development depends on cell-to-cell redistribution of the plant hormone auxin, which is facilitated by the plasma membrane (PM) localized PIN FORMED (PIN) proteins. Auxin export activity, developmental roles, subcellular trafficking, and polarity of PINs have been well studied, but their structure remains elusive besides a rough outline that they contain two groups of 5 alpha-helices connected by a large hydrophilic loop (HL). Here, we focus on the PIN1 HL as we could produce it in sufficient quantities for biochemical investigations to provide insights into its secondary structure. Circular dichroism (CD) studies revealed its nature as an intrinsically disordered protein (IDP), manifested by the increase of structure content upon thermal melting. Consistent with IDPs serving as interaction platforms, PIN1 loops homodimerize. PIN1 HL cytoplasmic overexpression in Arabidopsis disrupts early endocytic trafficking of PIN1 and PIN2 and causes defects in the cotyledon vasculature formation. In summary, we demonstrate that PIN1 HL has an intrinsically disordered nature, which must be considered to gain further structural insights. Some secondary structures may form transiently during pairing with known and yet-to-be-discovered interactors.

Návaznosti

EF18_046/0015974, projekt VaV

Název: Modernizace České infrastruktury pro integrativní strukturní biologii

90127, velká výzkumná infrastruktura

Název: CIISB II

90129, velká výzkumná infrastruktura

Název: Czech-BioImaging II

Citovat

BILANOVIČOVÁ, Veronika, Nikola RÝDZA, Lilla KOCZKA, Martin HESS, Elena FERARU, Jiri FRIML a Tomasz NODZYNSKI. The Hydrophilic Loop of Arabidopsis PIN1 Auxin Efflux Carrier Harbors Hallmarks of an Intrinsically Disordered Protein. International Journal of Molecular Sciences. Basel: Multidisciplinary Digital Publishing Institute, 2022, roč. 23, č. 11, s. 6352-6369. ISSN 1422-0067. Dostupné z: https://dx.doi.org/10.3390/ijms23116352.

@article{2248103,
   author = {Bilanovičová, Veronika and Rýdza, Nikola and Koczka, Lilla and Hess, Martin and Feraru, Elena and Friml, Jiri and Nodzynski, Tomasz},
   article_location = {Basel},
   article_number = {11},
   doi = {http://dx.doi.org/10.3390/ijms23116352},
   keywords = {PIN1; hydrophilic hoop; dimerization; intrinsic disorder; subcellular trafficking},
   language = {eng},
   issn = {1422-0067},
   journal = {International Journal of Molecular Sciences},
   title = {The Hydrophilic Loop of Arabidopsis PIN1 Auxin Efflux Carrier Harbors Hallmarks of an Intrinsically Disordered Protein},
   url = {https://www.mdpi.com/1422-0067/23/11/6352},
   volume = {23},
   year = {2022}
}

TY  - JOUR
ID  - 2248103
AU  - Bilanovičová, Veronika - Rýdza, Nikola - Koczka, Lilla - Hess, Martin - Feraru, Elena - Friml, Jiri - Nodzynski, Tomasz
PY  - 2022
TI  - The Hydrophilic Loop of Arabidopsis PIN1 Auxin Efflux Carrier Harbors Hallmarks of an Intrinsically Disordered Protein
JF  - International Journal of Molecular Sciences
VL  - 23
IS  - 11
SP  - 6352
EP  - 6352
PB  - Multidisciplinary Digital Publishing Institute
SN  - 14220067
KW  - PIN1
KW  - hydrophilic hoop
KW  - dimerization
KW  - intrinsic disorder
KW  - subcellular trafficking
UR  - https://www.mdpi.com/1422-0067/23/11/6352
N2  - Much of plant development depends on cell-to-cell redistribution of the plant hormone auxin, which is facilitated by the plasma membrane (PM) localized PIN FORMED (PIN) proteins. Auxin export activity, developmental roles, subcellular trafficking, and polarity of PINs have been well studied, but their structure remains elusive besides a rough outline that they contain two groups of 5 alpha-helices connected by a large hydrophilic loop (HL). Here, we focus on the PIN1 HL as we could produce it in sufficient quantities for biochemical investigations to provide insights into its secondary structure. Circular dichroism (CD) studies revealed its nature as an intrinsically disordered protein (IDP), manifested by the increase of structure content upon thermal melting. Consistent with IDPs serving as interaction platforms, PIN1 loops homodimerize. PIN1 HL cytoplasmic overexpression in Arabidopsis disrupts early endocytic trafficking of PIN1 and PIN2 and causes defects in the cotyledon vasculature formation. In summary, we demonstrate that PIN1 HL has an intrinsically disordered nature, which must be considered to gain further structural insights. Some secondary structures may form transiently during pairing with known and yet-to-be-discovered interactors.
ER  -

BILANOVIČOVÁ, Veronika, Nikola RÝDZA, Lilla KOCZKA, Martin HESS, Elena FERARU, Jiri FRIML a Tomasz NODZYNSKI. The Hydrophilic Loop of Arabidopsis PIN1 Auxin Efflux Carrier Harbors Hallmarks of an Intrinsically Disordered Protein. \textit{International Journal of Molecular Sciences}. Basel: Multidisciplinary Digital Publishing Institute, 2022, roč.~23, č.~11, s.~6352-6369. ISSN~1422-0067. Dostupné z: https://dx.doi.org/10.3390/ijms23116352.

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