The Library
The subcellular localization of tubby-like proteins and participation in stress signaling and root colonization by the mutualist piriformospora indica
Tools
Reitz, Marco U., Bissue, J. K., Zocher, K., Attard, A., Hückelhoven, Ralph, Becker, K., Imani, Jafargholi, Eichmann, Ruth and Schäfer, Patrick (2012) The subcellular localization of tubby-like proteins and participation in stress signaling and root colonization by the mutualist piriformospora indica. Plant Physiology, Volume 160 (Number 1). pp. 349-364. doi:10.1104/pp.112.201319 ISSN 0032-0889.
Research output not available from this repository.
Request-a-Copy directly from author or use local Library Get it For Me service.
Official URL: http://dx.doi.org/10.1104/pp.112.201319
Abstract
Tubby and Tubby-like proteins (TLPs) were first discovered in mammals, where they are involved in the development and function of neuronal cells. Due to their importance as plasma membrane (PM)-tethered transcription factors or mediators of vesicle trafficking, their lack causes obesity and other disease syndromes. Phosphatidylinositol 4,5-bisphosphate (PIP2)-binding of the C-terminal Tubby domain attaches these proteins to the PM and vesicles and is essential for function. TLPs are conserved across eukaryotic kingdoms including plants suggesting fundamental biological functions of TLPs. Plant TLPs possess an N-terminal F-box domain that distinguishes them from other eukaryotic TLPs. Arabidopsis thaliana encodes 11 AtTLPs that fall into six phylogenetic clades. We identified the significance of AtTLPs for root colonization of Arabidopsis by the mutualistic fungus Piriformospora indica. Our results further indicate conserved PIP2-binding sites in the TUBBY domains that are required for PM anchoring of AtTLPs. More detailed studies revealed phospholipase C-triggered release of AtTLP3 from the PM, indicating a conserved mechanism as reported for mammalian Tubby and TLP3. We further show that H2O2 stimulates release of AtTLP3 from the PM, presumably for activating downstream events. Different from mammalian homologues, the N-terminal part of almost all AtTLPs has nucleo-cytosolic and plastidial localization patterns. Thus, it is tempting to assume that TLPs translate reactive oxygen species currents into signaling not only for transcriptional regulation in the nucleus, but also affect plastid-associated functions after release from the PM.
Item Type: | Journal Article | ||||
---|---|---|---|---|---|
Divisions: | Faculty of Science, Engineering and Medicine > Science > Life Sciences (2010- ) | ||||
Journal or Publication Title: | Plant Physiology | ||||
Publisher: | American Society of Plant Biologists | ||||
ISSN: | 0032-0889 | ||||
Official Date: | 2012 | ||||
Dates: |
|
||||
Volume: | Volume 160 | ||||
Number: | Number 1 | ||||
Page Range: | pp. 349-364 | ||||
DOI: | 10.1104/pp.112.201319 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access |
Request changes or add full text files to a record
Repository staff actions (login required)
View Item |