Brassinosteroid nuclear signaling recruits HSP90 activity

Bibliographische Detailangaben
Veröffentlicht in:	The New phytologist. - 1979. - 203(2014), 3 vom: 08. Aug., Seite 743-57
1. Verfasser:	Samakovli, Despina (VerfasserIn)
Weitere Verfasser:	Margaritopoulou, Theoni, Prassinos, Constantinos, Milioni, Dimitra, Hatzopoulos, Polydefkis
Format:	Online-Aufsatz
Sprache:	English
Veröffentlicht:	2014
Zugriff auf das übergeordnete Werk:	The New phytologist
Schlagworte:	Journal Article Research Support, Non-U.S. Gov't Arabidopsis thaliana BIN2 brassinosteroid signaling gene expression heat shock protein 90 (HSP90) Arabidopsis Proteins Benzoquinones Brassinosteroids mehr... HSP90 Heat-Shock Proteins Hsp90-1 protein, Arabidopsis Hsp90-3 protein, Arabidopsis Lactams, Macrocyclic Protein Sorting Signals Protein Kinases EC 2.7.- BIN2 protein, Arabidopsis EC 2.7.1.- geldanamycin Z3K3VJ16KU

Beschreibung
Zusammenfassung:	© 2014 The Authors. New Phytologist © 2014 New Phytologist Trust. Heat shock protein 90 (HSP90) controls a number of developmental circuits, and serves a sophisticated and highly regulatory function in signaling pathways. Brassinosteroids (BRs) control many aspects of plant development. Genetic, physiological, cytological, gene expression, live cell imaging, and pharmacological approaches provide conclusive evidence for HSP90 involvement in Arabidopsis thalianaBR signaling. Nuclear-localized HSP90s translocate to cytoplasm when their activity is blocked by the HSP90 inhibitor geldanamycin (GDA). GDA treatment promoted the export of BIN2, a regulator of BR signaling, from the nucleus into the cytoplasm, indicating that active HSP90 is required to sustain BIN2 in the nucleus. HSP90 nuclear localization was inhibited by brassinolide (BL). HSP90s interact with BIN2 in the nucleus of untreated cells and in the cytoplasm of BL-treated cells, showing that the site-specific action of HSP90 on BIN2 is controlled by BRs. GDA and BL treatments change the expression of a common set of previously identified BR-responsive genes. This highlights the effect of active HSP90s on the regulation of BR-responsive genes. Our observations reveal that HSP90s have a central role in sustaining BIN2 nuclear function. We propose that BR signaling is mediated by HSP90 activity and via trafficking of BIN2-HSP90 complexes into the cytoplasm
Beschreibung:	Date Completed 30.03.2015 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE
ISSN:	1469-8137
DOI:	10.1111/nph.12843