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Dysregulation of these processes is implicated in numerous diseases, including cancer, liver disorders, and neurodegenerative diseases. p62\/Sequestosome 1 (SQSTM1) is a multifunctional protein that plays a central role in protein homeostasis and stress responses by regulating autophagy and signal transduction pathways. Through its multiple protein\u2010interacting domains, p62 functions both as a scaffold for selective autophagic degradation and as a signaling hub. Since our previous review of p62 a decade ago, substantial progress has been made in elucidating its molecular functions and physiological roles. Notably, p62 undergoes liquid\u2013liquid phase separation with ubiquitinated proteins to form membraneless condensates, termed p62 bodies, when cells are exposed to proteotoxic stress. By sequestering specific proteins, p62 bodies act as platforms for autophagy\u2010dependent degradation and stress signaling. These findings have substantially revised our view of p62 function, which was previously considered primarily as a receptor simply linking ubiquitinated substrates to autophagic membranes and connecting signaling molecules. This conceptual shift from one\u2010to\u2010one molecular interactions to multivalent, multimolecular, higher\u2010order assemblies has fundamentally redefined the functional landscape of p62. In this review, we highlight how p62 bodies integrate selective autophagy and stress signaling, with a particular emphasis on their emerging roles in disease pathogenesis and their potential as therapeutic targets.<\/jats:p>","DOI":"10.1111\/febs.70689","type":"journal-article","created":{"date-parts":[[2026,8,11]],"date-time":"2026-08-11T07:12:49Z","timestamp":1786432369000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["p62\/\n                    <scp>SQSTM1<\/scp>\n                    : From an autophagy receptor to a condensate organizer of selective autophagy and stress signaling"],"prefix":"10.1111","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3361-6314","authenticated-orcid":false,"given":"Jun\u2010ichi","family":"Sakamaki","sequence":"first","affiliation":[{"name":"Department of Physiology Juntendo University Graduate School of Medicine  Tokyo Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7672-7722","authenticated-orcid":false,"given":"Masaaki","family":"Komatsu","sequence":"additional","affiliation":[{"name":"Department of Physiology Juntendo University Graduate School of Medicine  Tokyo Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,8,11]]},"reference":[{"key":"e_1_2_13_2_1","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1016\/j.molcel.2019.09.005","article-title":"A diversity of selective autophagy receptors determines the specificity of the autophagy pathway","volume":"76","author":"Kirkin V","year":"2019","journal-title":"Mol Cell"},{"key":"e_1_2_13_3_1","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1146\/annurev-cellbio-120219-035530","article-title":"Mechanisms of selective autophagy","volume":"37","author":"Lamark T","year":"2021","journal-title":"Annu Rev Cell Dev 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