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Dhar, Souvik,Kim, Hyoujin,Segonzac, Cecile,Lee, Ji-Young Korean Society for Molecular and Cellular Biology 2021 Molecules and cells Vol.44 No.11
When perceiving microbe-associated molecular patterns (MAMPs) or plant-derived damage-associated molecular patterns (DAMPs), plants alter their root growth and development by displaying a reduction in the root length and the formation of root hairs and lateral roots. The exogenous application of a MAMP peptide, flg22, was shown to affect root growth by suppressing meristem activity. In addition to MAMPs, the DAMP peptide PEP1 suppresses root growth while also promoting root hair formation. However, the question of whether and how these elicitor peptides affect the development of the vascular system in the root has not been explored. The cellular receptors of PEP1, PEPR1 and PEPR2 are highly expressed in the root vascular system, while the receptors of flg22 (FLS2) and elf18 (EFR) are not. Consistent with the expression patterns of PEP1 receptors, we found that exogenously applied PEP1 has a strong impact on the division of stele cells, leading to a reduction of these cells. We also observed the alteration in the number and organization of cells that differentiate into xylem vessels. These PEP1-mediated developmental changes appear to be linked to the blockage of symplastic connections triggered by PEP1. PEP1 dramatically disrupts the symplastic movement of free green fluorescence protein (GFP) from phloem sieve elements to neighboring cells in the root meristem, leading to the deposition of a high level of callose between cells. Taken together, our first survey of PEP1-mediated vascular tissue development provides new insights into the PEP1 function as a regulator of cellular reprogramming in the Arabidopsis root vascular system.
Structural Basis for Assembly and Function of a Heterodimeric Plant Immune Receptor
Williams, Simon J.,Sohn, Kee Hoon,Wan, Li,Bernoux, Maud,Sarris, Panagiotis F.,Segonzac, Cecile,Ve, Thomas,Ma, Yan,Saucet, Simon B.,Ericsson, Daniel J.,Casey, Lachlan W.,Lonhienne, Thierry,Winzor, Dona American Association for the Advancement of Scienc 2014 Science Vol.344 No.6181
<P><B>Universal Immune Function</B></P><P>Certain pathogen effectors are detected in plants by cytoplasmic receptors. First solving the crystal structures of <I>Arabidopsis</I> receptors, <B>Williams <I>et al.</I></B> (p. 299; see the Perspective by <B>Nishimura and Dangl</B>) discovered that in the resting state, the structures form a heterodimer that readies the complex for effector binding and keeps the signaling domains from firing too early. Once the pathogen effector binds, the structure of the complex shifts such that the signaling domains can form a homodimer to initiate downstream signaling. Similarities between these plant-pathogen receptors and Toll-like receptors in animals suggest the molecular mechanisms may translate broadly.</P>