KinG Is a Plant-Specific Kinesin That Regulates Both Intra- and Intercellular Movement of SHORT-ROOT

• Published in: Plant physiology (Bethesda) 2018-01, Vol.176 (1), p.392-405
• Main Authors: Spiegelman, Ziv, Lee, Chin-Mei, Gallagher, Kimberly L.
• Format: Article
• Language: English
• Subjects: Actins - metabolism; Arabidopsis - metabolism; Arabidopsis Proteins - chemistry; Arabidopsis Proteins - metabolism; Bridged Bicyclo Compounds, Heterocyclic - pharmacology; Dinitrobenzenes - pharmacology; Endosomes - metabolism; Extracellular Space - metabolism; FOCUS ISSUE; Intracellular Space - metabolism; Kinesins - chemistry; Kinesins - metabolism; Meristem - metabolism; Microtubules - metabolism; Models, Biological; Mutation - genetics; Nicotiana - cytology; Plant Epidermis - cytology; Plant Leaves - cytology; Plant Roots - metabolism; Protein Domains; Protein Transport; Species Specificity; Subcellular Fractions - metabolism; Sulfanilamides - pharmacology; Thiazolidines - pharmacology; Transcription Factors - metabolism
• ISSN: 0032-0889; 1532-2548
• DOI: 10.1104/pp.17.01518

Both endogenous plant proteins and viral movement proteins associate with microtubules to promote their movement through plasmodesmata. The association of viral movement proteins with microtubules facilitates the formation of virus-associated replication complexes, which are required for the amplification and subsequent spread of the virus. However, the role of microtubules in the intercellular movement of plant proteins is less clear. Here we show that the SHORT-ROOT (SHR) protein, which moves between cells in the root to regulate root radial patterning, interacts with a type-14 kinesin, KINESIN G (KinG). KinG is a calponin homology domain kinesin that directly interacts with the SHR-binding protein SIEL (SHR-INTERACING EMBRYONIC LETHAL) and localizes to both microtubules and actin. Since SIEL and SHR associate with endosomes, we suggest that KinG serves as a linker between SIEL, SHR, and the plant cytoskeleton. Loss of KinG function results in a decrease in the intercellular movement of SHR and an increase in the sensitivity of SHR movement to treatment with oryzalin. Examination of SHR and KinG localization and dynamics in live cells suggests that KinG is a nonmotile kinesin that promotes the pausing of SHR-associated endosomes. We suggest a model in which interaction of KinG with SHR allows for the formation of stable movement complexes that facilitate the cell-to-cell transport of SHR.