Graduate research assistant Purdue University West Lafayette, Indiana
Body of Abstract: Protein-protein interactions play a crucial role in driving cellular processes and enabling appropriate physiological responses in organisms. The plant hormone ethylene signaling pathway is complex and regulated by the spatiotemporal regulation of its signaling molecules. Constitutive Triple Response 1 (CTR1), a key negative regulator of the pathway, regulates the function of Ethylene-Insensitive 2 (EIN2), a positive regulator of ethylene signaling, at the endoplasmic reticulum (ER) through phosphorylation. Our recent study revealed CTR1 can also move from the ER to the nucleus in response to ethylene and positively regulate ethylene responses by stabilizing EIN3. To gain more insights into the role of CTR1 in plants, we used TurboID proximity labeling and mass spectrometry to identify the proximal proteomes of CTR1 that were transiently expressed in N. benthamiana. The identified proximal proteins include known ethylene signaling components as well as proteins involved in diverse cellular processes such as carbon metabolism, gene expression, and organelle organization. Our study demonstrates the feasibility of proximity labeling using the N. benthamiana transient expression system and identifies the potential interactors of CTR1 in vivo, suggesting the role of CTR1 in a wide range of cellular processes.