Schwann cells are critical for the proper development and function of the peripheral nervous system, where they form a collaborative relationship with axons. Past studies highlighted that a pair of proteins called the prohibitins play major roles in Schwann cell biology. Prohibitins are ubiquitously expressed and versatile proteins. We have previously shown that while prohibitins play a crucial role in Schwann cell mitochondria for long-term myelin maintenance and axon health, they may also be present at the Schwann cell-axon interface during development. The current data set uses BioID to identify a pool of candidate PHB2 interactors in Schwann cells and explores how the PHB2 interactome changes depending on neuronal signals. We expressed a PHB2-turboID fusion construct in primary rat Schwann cells; turboID is a 35 kDa engineered biotin ligase that rapidly biotinylates proximal proteins. Thus, proteins interacting with PHB2-turboID within an approximately 10 nm radius are tagged with biotin. As a control, primary rat Schwann cells were transfected with an unfused turboID construct (Con-turboID). Schwann cells expressing Con-turboID or PHB2-turboID were plated alone or onto primary rat DRG neurons, in the presence or absence of biotin. After 2 hours, proteins were harvested from the cultures and biotinylated proteins were purified using streptavidin-affinity purification (AP). We then used liquid chromatography-mass spectrometry (LC-MS) to identify the PHB2-turboID interactors (the biotinylated proteins) in our purified pool. The PHB2 interactors identified here, especially those which increase or decrease interaction with PHB2-turboID in the presence of neurons, may play a role in prohibitin-associated Schwann cell-axon communication.