Novel ABP1-TMK auxin sensing system controls ROP GTPase-mediated interdigitated cell expansion in Arabidopsis.

ROP GTPases (Rho-like GTPase from plants), plant counterparts of animal and fungal Rho-family GTPases, have recently been shown to be key components of a novel signaling pathway activated by the plant hormone auxin. Auxin (indole acetic acid) is a key regulator of virtually every aspect of plant growth and development, yet the molecular mechanisms of auxin responses remain largely unknown. AUXIN BINDING PROTEIN1 (ABP1) is an ancient protein that binds auxin and has been implied as a receptor for a number of auxin responses, but its precise mechanism remains unresolved. A paradox for ABP1's action is that it is predominantly found in the endoplasmic reticulum (ER) lumen, while it has been implicated as a cell surface auxin receptor, functionally distinct from the nuclear TIR1/AFB auxin receptor family that regulates transcriptional responses. Since our group reported that ABP1 is required for activating two antagonizing ROP signaling pathways involved in cytoskeletal reorganization and cell shape formation in Arabidopsis leaf pavement cells, we recently further showed that the plasma membrane-localized TMK receptor-like kinases functionally interact in a complex with ABP1 and are required for ABP1-dependent activation of ROP GTPases by auxin. The formation of this cell surface complex is induced by auxin and requires functional ABP1. These exciting findings provide convincing evidence for this novel auxin sensing system on the cell surface and suggest intriguing mechanisms for TMKs being functional partners of ABP1 to transmit extracellular auxin signal to intracellular ROP signaling module during polar cell expansion.