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Understanding the molecular regulation of autophagy is critical for developing interventional approaches for cancer therapy. In this study, we report that migfilin, a focal adhesion protein, plays a novel role in promoting autophagy by increasing autophagosome\u2013lysosome fusion. We found that migfilin is associated with SNAP29 and Vamp8, thereby facilitating Stx17-SNAP29-Vamp8 SNARE complex assembly. Depletion of migfilin disrupted the formation of the SNAP29-mediated SNARE complex, which consequently blocked the autophagosome-lysosome fusion, ultimately suppressing cancer cell growth. Restoration of the SNARE complex formation rescued migfilin-deficiency\u2013induced autophagic flux defects. Finally, we found depletion of migfilin inhibited cancer cell proliferation. SNARE complex reassembly successfully reversed migfilin-deficiency\u2013induced inhibition of cancer cell growth. Taken together, our study uncovers a new function of migfilin as an autophagy-regulatory protein and suggests that targeting the migfilin\u2013SNARE assembly could provide a promising therapeutic approach to alleviate cancer progression.<\/jats:p>","DOI":"10.1083\/jcb.202312119","type":"journal-article","created":{"date-parts":[[2024,7,19]],"date-time":"2024-07-19T02:20:57Z","timestamp":1721355657000},"update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":10,"title":["Migfilin promotes autophagic flux through direct interaction with SNAP29 and Vamp8"],"prefix":"10.1083","volume":"223","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6327-4023","authenticated-orcid":true,"given":"Renwei","family":"Cai","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/049tv2d57","id-type":"ROR","asserted-by":"publisher"}],"name":"School of Life Sciences, Guangdong Provincial Key Laboratory of Cell Microenvironment and Disease 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