{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,16]],"date-time":"2026-01-16T01:33:15Z","timestamp":1768527195173,"version":"3.49.0"},"reference-count":136,"publisher":"MDPI AG","issue":"10","license":[{"start":{"date-parts":[[2023,10,15]],"date-time":"2023-10-15T00:00:00Z","timestamp":1697328000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Japan Society for the Promotion of Science","award":["KAKENHI 23K10424"],"award-info":[{"award-number":["KAKENHI 23K10424"]}]},{"name":"Japan Society for the Promotion of Science","award":["KAKENHI 21K11275"],"award-info":[{"award-number":["KAKENHI 21K11275"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Genes"],"abstract":"<jats:p>The protein 4.1 and membrane palmitoylated protein (MPP) families were originally found as components in the erythrocyte membrane skeletal protein complex, which helps maintain the stability of erythrocyte membranes by linking intramembranous proteins and meshwork structures composed of actin and spectrin under the membranes. Recently, it has been recognized that cells and tissues ubiquitously use this membrane skeletal system. Various intramembranous proteins, including adhesion molecules, ion channels, and receptors, have been shown to interact with the 4.1 and MPP families, regulating cellular and tissue dynamics by binding to intracellular signal transduction proteins. In this review, we focus on our previous studies regarding genetically modified animal models, especially on 4.1G, MPP6, and MPP2, to describe their functional roles in the peripheral nervous system, the central nervous system, the testis, and bone formation. As the membrane skeletal proteins are located at sites that receive signals from outside the cell and transduce signals inside the cell, it is necessary to elucidate their molecular interrelationships, which may broaden the understanding of cell and tissue functions.<\/jats:p>","DOI":"10.3390\/genes14101942","type":"journal-article","created":{"date-parts":[[2023,10,15]],"date-time":"2023-10-15T10:47:32Z","timestamp":1697366852000},"page":"1942","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Recent Progress on Genetically Modified Animal Models for Membrane Skeletal Proteins: The 4.1 and MPP Families"],"prefix":"10.3390","volume":"14","author":[{"given":"Nobuo","family":"Terada","sequence":"first","affiliation":[{"name":"Health Science Division, Department of Medical Sciences, Shinshu University Graduate School of Medicine, Science and Technology, Matsumoto City, Nagano 390-8621, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yurika","family":"Saitoh","sequence":"additional","affiliation":[{"name":"Health Science Division, Department of Medical Sciences, Shinshu University Graduate School of Medicine, Science and Technology, Matsumoto City, Nagano 390-8621, Japan"},{"name":"Center for Medical Education, Teikyo University of Science, Adachi-ku, Tokyo 120-0045, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7259-4248","authenticated-orcid":false,"given":"Masaki","family":"Saito","sequence":"additional","affiliation":[{"name":"School of Pharma-Science, Teikyo University, Itabashi-ku, Tokyo 173-8605, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tomoki","family":"Yamada","sequence":"additional","affiliation":[{"name":"Health Science Division, Department of Medical Sciences, Shinshu University Graduate School of Medicine, Science and Technology, Matsumoto City, Nagano 390-8621, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Akio","family":"Kamijo","sequence":"additional","affiliation":[{"name":"Health Science Division, Department of Medical Sciences, Shinshu University Graduate School of Medicine, Science and Technology, Matsumoto City, Nagano 390-8621, Japan"},{"name":"Division of Basic & Clinical Medicine, Nagano College of Nursing, Komagane City, Nagano 399-4117, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9938-6569","authenticated-orcid":false,"given":"Takahiro","family":"Yoshizawa","sequence":"additional","affiliation":[{"name":"Division of Animal Research, Research Center for Advanced Science and Technology, Shinshu University, Matsumoto City, Nagano 390-8621, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1225-1902","authenticated-orcid":false,"given":"Takeharu","family":"Sakamoto","sequence":"additional","affiliation":[{"name":"Department of Cancer Biology, Institute of Biomedical Science, Kansai Medical University, Hirakata City, Osaka 573-1010, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2023,10,15]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1182\/blood-2014-12-512772","article-title":"Anatomy of the red cell membrane skeleton: Unanswered questions","volume":"127","author":"Lux","year":"2016","journal-title":"Blood"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/j.bbamem.2013.05.030","article-title":"The Protein 4.1 family: Hub proteins in animals for organizing membrane proteins","volume":"1838","author":"Baines","year":"2014","journal-title":"Biochim. 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