English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  The C2-domain protein QUIRKY and the atypical receptor-like kinase STRUBBELIG localize to plasmodesmata and mediate tissue morphogenesis in Arabidopsis thaliana

Vaddepalli, P., Yashodar, B., Hillmer, S., Robinson, D., & Schneitz, K. (2013). The C2-domain protein QUIRKY and the atypical receptor-like kinase STRUBBELIG localize to plasmodesmata and mediate tissue morphogenesis in Arabidopsis thaliana. In 24th International Conference on Arabidopsis Research (ICAR 2013) (pp. 19).

Item is

Basic

show hide
Genre: Meeting Abstract

Files

show Files

Locators

show
hide
Description:
-
OA-Status:
Not specified

Creators

show
hide
 Creators:
Vaddepalli, P, Author
Yashodar, B1, Author           
Hillmer, S, Author
Robinson, DG, Author
Schneitz, K, Author
Affiliations:
1Department Cell Biology, Max Planck Institute for Developmental Biology, Max Planck Society, ou_3375717              

Content

show
hide
Free keywords: -
 Abstract: Tissue morphogenesis in plants requires the coordination of cellular behavior within and across clonally distinct histogenic layers. In Arabidopsis, the leucine-rich repeat receptor-like kinase STRUBBELIG (SUB) is required for inter-cell-layer communication during floral and ovule development. SUB is an atypical receptor-like kinase that when mutated, shows defects in floral organ, stem and silique shape, ovule integument morphogenesis and root hair patterning. SUB affects tissue morphogenesis in a non cell-autonomous manner thus influencing the behavior of neighboring cells. QUIRKY (QKY), ZERZAUST (ZET) and ANGUSTIFOLIA (AN) belong to STRUBBELIG-LIKE MUTANT (SLM) class of genes, proposed to contribute to SUB-dependent signal transduction. In the present work, molecular characterization of QKY was undertaken with the main focus on its role in SUB mediated signaling. Mapping and molecular identification of QKY revealed that it encodes a novel multiple C2 domain-containing transmembrane protein (MCTP). Biochemical studies imply that QKY binds to phospholipids in a Ca+2 dependent manner. Protein localization experiments indicate that QKY is specifically associated with plasmodesmata (PD). Immunogold electron microscopy results confirm the PD localization of QKY and also reveal the previously unknown PD localization of SUB. SUB and QKY do not appear to be involved in non-selective movement GFP-sized proteins. Yeast-two-hybrid data indicate that SUB and QKY can interact directly. Thus, the data imply that SUB signaling mediates tissue morphogenesis by influencing selective transport of molecules through PD.

Details

show
hide
Language(s):
 Dates: 2013-06
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: -
 Degree: -

Event

show
hide
Title: 24th International Conference on Arabidopsis Research (ICAR 2013)
Place of Event: Sydney, Australia
Start-/End Date: 2013-06-24 - 2013-06-28

Legal Case

show

Project information

show

Source 1

show
hide
Title: 24th International Conference on Arabidopsis Research (ICAR 2013)
Source Genre: Proceedings
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: - Sequence Number: SYM-03-04 Start / End Page: 19 Identifier: -