Stress granules (SGs) are dynamic, phase-separated assemblies that form in response to cellular stress and must be efficiently cleared to restore homeostasis. While both reversible disassembly and autophagy-mediated degradation have been implicated in SG clearance, the molecular mechanisms that determine SG fate remain poorly defined. Here, we propose that the deubiquiting enzyme DUBXX functions as a gatekeeper of SG clearance by fine-tuning K63-linked ubiquitination of the SG scaffold protein G3BP1. Upon acute stress, DUBXX is recruited to SGs and selectively trims K63-linked ubiquitin chains on G3BP1, preventing excessive ubiquitin accumulation while preserving an extraction-competent ubiquitin architecture. This controlled ubiquitination facilitates productive engagement of the AAA+ ATPase VCP, promoting efficient extraction of SG components and driving SG disassembly during stress recovery. In contrast, loss of DUBXX function in prolonged stress leads to persistent K63-linked ubiquitination of G3BP1, impaired VCP-mediated extraction, and SG stabilization. These mature SGs are subsequently diverted toward autophagy-dependent clearance rather than reversible disassembly. Together, this model identifies DUBXX-mediated ubiquitin trimming as a key regulatory checkpoint that determines SG fate and highlights K63-linked ubiquitin architecture as a decisive signal governing the balance between SG disassembly and degradation.