The Hydrophilic Loop of
PIN1
dimerization
hydrophilic hoop
intrinsic disorder
subcellular trafficking
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
06 Jun 2022
06 Jun 2022
Historique:
received:
13
04
2022
revised:
31
05
2022
accepted:
04
06
2022
entrez:
10
6
2022
pubmed:
11
6
2022
medline:
14
6
2022
Statut:
epublish
Résumé
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
Identifiants
pubmed: 35683031
pii: ijms23116352
doi: 10.3390/ijms23116352
pmc: PMC9181416
pii:
doi:
Substances chimiques
Arabidopsis Proteins
0
Indoleacetic Acids
0
Intrinsically Disordered Proteins
0
Membrane Transport Proteins
0
PIN1 protein, Arabidopsis
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Austrian Science Fund FWF
ID : V 690
Pays : Austria
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