Other formats:
BibTeX
LaTeX
RIS
@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 and 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, vol.~23, No~11, p.~6352-6369. ISSN~1422-0067. Available from: https://dx.doi.org/10.3390/ijms23116352.
|
