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In the skin, the ECM supports tissue integrity while also controlling processes such as stem cell maintenance, wound healing and disease progression. This review focuses on laminin\u2010332, a key component of the epidermal\u2013dermal junction. Its essential role in maintaining epidermal cohesion is illustrated by junctional epidermolysis bullosa, a severe inherited blistering disorder and recent advances in laminin\u2010332\u2010targeted genetic therapies are discussed. Beyond structural support, laminin\u2010332 also mediates signalling through integrins and syndecans, thereby influencing epidermal homeostasis, migration, repair and the development of cutaneous squamous cell carcinoma. Its role in epidermal stem cell maintenance further links laminin\u2010332 to skin ageing. The review also examines its functions in hair follicle biology, melanocyte behaviour, skin immunity and emerging evidence implicating laminin\u2010332 in epidermal metabolism\u2014an exciting area for future investigation. Finally, the structure and functions of other cutaneous laminins are compared with laminin\u2010332 to help explain its specialised roles.<\/jats:p>","DOI":"10.1111\/exd.70293","type":"journal-article","created":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T05:47:52Z","timestamp":1781070472000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["So Much More Than Just Structural Support: Laminin\u2010332 and Its Multifaceted Functions in Skin Homeostasis and Disease"],"prefix":"10.1111","volume":"35","author":[{"ORCID":"https:\/\/orcid.org\/0009-0001-7572-6581","authenticated-orcid":false,"given":"Piotr","family":"Parzymies","sequence":"first","affiliation":[{"name":"Centre for Cell Biology and Cutaneous Research, Blizard Institute Queen Mary University of London  London UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2026,6,9]]},"reference":[{"key":"e_1_2_16_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41580-024-00767-3"},{"key":"e_1_2_16_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.semcdb.2022.02.027"},{"key":"e_1_2_16_4_1","doi-asserted-by":"publisher","DOI":"10.1101\/cshperspect.a005124"},{"key":"e_1_2_16_5_1","doi-asserted-by":"publisher","DOI":"10.3390\/ijms19041003"},{"key":"e_1_2_16_6_1","doi-asserted-by":"publisher","DOI":"10.1093\/oxfordjournals.jbchem.a021541"},{"key":"e_1_2_16_7_1","doi-asserted-by":"publisher","DOI":"10.3390\/biom10121607"},{"key":"e_1_2_16_8_1","doi-asserted-by":"publisher","DOI":"10.1111\/exd.13446"},{"key":"e_1_2_16_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.matbio.2005.05.006"},{"key":"e_1_2_16_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.semcancer.2019.09.026"},{"issue":"3","key":"e_1_2_16_11_1","first-page":"295","article-title":"Basement Membrane Proteins Kalinin and Nicein Are Structurally and Immunologically Identical","volume":"69","author":"Marinkovich M. 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