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Comment
. 2018 May;23(5):372-374.
doi: 10.1016/j.tplants.2018.03.008. Epub 2018 Mar 27.

The APEX Approaches: A Unified LRR-RK Network Revealed

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Comment

The APEX Approaches: A Unified LRR-RK Network Revealed

Yanyan Huang et al. Trends Plant Sci. 2018 May.

Abstract

Leucine-rich repeat receptor kinases (LRR-RKs) represent a large and functionally diverse family of transmembrane proteins critical for signal recognition and transduction at the plant cell plasma membrane. Here, we discuss a recent report which used a systems-level approach to validate key paradigms by constructing an LRR-RK interaction network model.

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Figures

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APEX as a connector of receptor subnetworks.
The short LRR-RK APEX (center; red), was demonstrated to act as an articulation point in the LRR-RK cell-surface interaction network. The interconnectedness of the various receptor subnetworks (represented top left/right) was predicted to largely rely on APEX and short LRR-RKs like it. APEX likely acts in a manner similar to BAK1 by complexing with several LRR-RKs (represented left/right; green/blue) or indirectly affecting the integrity of other subnetworks. Examples of features which govern the interaction specificity and affinity for the formation of these co-receptor complexes (ligand-induced heterodimerization, transmembrane-helix interactions, intracellular kinase trans-phosphorylation) are labeled throughout the figure. The illustrated LRR-RK models do not represent true molecular structures.

Comment on

  • An extracellular network of Arabidopsis leucine-rich repeat receptor kinases.
    Smakowska-Luzan E, Mott GA, Parys K, Stegmann M, Howton TC, Layeghifard M, Neuhold J, Lehner A, Kong J, Grünwald K, Weinberger N, Satbhai SB, Mayer D, Busch W, Madalinski M, Stolt-Bergner P, Provart NJ, Mukhtar MS, Zipfel C, Desveaux D, Guttman DS, Belkhadir Y. Smakowska-Luzan E, et al. Nature. 2018 Jan 18;553(7688):342-346. doi: 10.1038/nature25184. Epub 2018 Jan 10. Nature. 2018. PMID: 29320478 Free PMC article.

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