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Published on October 20, 2006; 10.1104/pp.106.088716

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Received August 25, 2006
Accepted October 13, 2006

Molecular Interactions of Arabinogalactan-proteins (AGPs) with Cortical Microtubules and F-actin in Bright Yellow-2 (BY-2) Tobacco Cultured Cells

Harjinder Singh Sardar , Jie Yang , and Allan M. Showalter *

Department of Environmental and Plant Biology, Ohio University, Athens, OH 45701-2979.; Molecular and Cellular Biology Program, Ohio University, Athens, OH 45701-2979.

* Corresponding author; email: showalte{at}ohio.edu.

Arabinogalactan-proteins (AGPs), a superfamily of plant hydroxyproline-rich glycoproteins, are present at cell surfaces. Although precise functions of AGPs remain elusive, they are widely implicated in plant growth and development. A well characterized classical tomato AGP containing a glycosylphophatidylinositol (GPI) plasma membrane anchor sequence was used here to elucidate functional roles of AGPs. Transgenic tobacco BY-2 (Nicotiana tobaccum) cells stably expressing GFP-LeAGP-1 were plasmolysed and used to localize LeAGP-1 on the plasma membrane and in Hechtian strands. Cytoskeleton disruptors and {beta}-Yariv reagent (which binds and perturbs AGPs) were used to examine the role of LeAGP-1 as a candidate linker protein between the plasma membrane and cytoskeleton. This study used a two-pronged approach. First, BY-2 cells, either WT or expressing GFP-MBD (microtubule binding domain), were treated with {beta}-Yariv reagent and effects on microtubules (MTs) and F-actin were observed. Second, BY-2 cells expressing GFP-LeAGP-1 were treated with amiprophosmethyl (APM) and cytochalasin-D, to disrupt MTs and F-actin, and effects on LeAGP-1 localization were observed. {beta}-Yariv treatment resulted in terminal cell bulging, puncta formation and depolymerization/disorganization of MTs, indicating a likely role for AGPs in cortical MT organization. {beta}-Yariv treatment also resulted in the formation of thicker actin filaments, indicating a role for AGPs in actin polymerization. Similarly, APM and cytochalasin-D treatments resulted in relocalization of LeAGP-1 on Hechtian strands and indicate roles for MTs and F-actin in AGP organization at the cell surface and in Hechtian strands. Collectively, these studies indicate that GPI-anchored AGPs function to link the plasma membrane to the cytoskeleton.




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