Salt stress-induced disassembly of Arabidopsis cortical microtubule arrays involves 26S proteasome-dependent degradation of SPIRAL1.
Songhu Wang, Jasmina Kurepa, Takashi Hashimoto, Jan A Smalle
Index: Plant Cell 23(9) , 3412-27, (2011)
Full Text: HTML
Abstract
The dynamic instability of cortical microtubules (MTs) (i.e., their ability to rapidly alternate between phases of growth and shrinkage) plays an essential role in plant growth and development. In addition, recent studies have revealed a pivotal role for dynamic instability in the response to salt stress conditions. The salt stress response includes a rapid depolymerization of MTs followed by the formation of a new MT network that is believed to be better suited for surviving high salinity. Although this initial depolymerization response is essential for the adaptation to salt stress, the underlying molecular mechanism has remained largely unknown. Here, we show that the MT-associated protein SPIRAL1 (SPR1) plays a key role in salt stress-induced MT disassembly. SPR1, a microtubule stabilizing protein, is degraded by the 26S proteasome, and its degradation rate is accelerated in response to high salinity. We show that accelerated SPR1 degradation is required for a fast MT disassembly response to salt stress and for salt stress tolerance.
Related Compounds
Related Articles:
Isolation of a protein interacting with Vfphot1a in guard cells of Vicia faba.
2005-07-01
[Plant Physiol. 138(3) , 1615-26, (2005)]
Change in the actin cytoskeleton during seismonastic movement of Mimosa pudica.
2006-04-01
[Plant Cell Physiol. 47(4) , 531-9, (2006)]
Localization of actin filaments on mitotic apparatus in tobacco BY-2 cells.
2005-09-01
[Planta 222(1) , 118-29, (2005)]
2005-12-01
[Protoplasma 226(3-4) , 169-74, (2005)]
Involvement of microtubules in rhizoid differentiation of Spirogyra species.
2003-06-01
[Protoplasma 221(3-4) , 227-35, (2003)]