FERONIA (FER), a receptor-like kinase involved in plant immunity, cell expansion, and mechanical signal transduction, is known to be endocytosed and degraded in response to treatment with its peptide ligand RAPID ALKALINIZATION FACTOR 1 (RALF1). Using confocal fluorescence microscopy and biochemical assays, we have found that full length FER-eGFP abundance at the plasma membrane is also regulated by mechanical stimulation, but through a separate, cysteine protease-dependent pathway. Like RALF1 treatment, both mechanical bending and mechanical wounding trigger a reduction in plasma membrane-localized, native promoter-driven FER-eGFP in Arabidopsis roots, hypocotyls, and cotyledons. However, pharmacological inhibition of protein trafficking and degradation suggests that while RALF1 induces clathrin-mediated endocytosis and subsequent degradation of FER-eGFP, mechanical stimulation triggers cleavage and/or degradation of FER-eGFP in a cysteine protease-dependent, clathrin-independent manner. Despite the stimulus-dependent differences in these two pathways, we found that both require early FER signaling components, including Ca2+ signaling, FER kinase activity, and the presence of LLG1, a FER-interacting protein with an essential role in FER-dependent signal transduction.