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Recent Progress on Genetically Modified Animal Models for Membrane Skeletal Proteins: The 4.1 and MPP Families
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 sp...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10606877/ https://www.ncbi.nlm.nih.gov/pubmed/37895291 http://dx.doi.org/10.3390/genes14101942 |
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author | Terada, Nobuo Saitoh, Yurika Saito, Masaki Yamada, Tomoki Kamijo, Akio Yoshizawa, Takahiro Sakamoto, Takeharu |
author_facet | Terada, Nobuo Saitoh, Yurika Saito, Masaki Yamada, Tomoki Kamijo, Akio Yoshizawa, Takahiro Sakamoto, Takeharu |
author_sort | Terada, Nobuo |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-10606877 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-106068772023-10-28 Recent Progress on Genetically Modified Animal Models for Membrane Skeletal Proteins: The 4.1 and MPP Families Terada, Nobuo Saitoh, Yurika Saito, Masaki Yamada, Tomoki Kamijo, Akio Yoshizawa, Takahiro Sakamoto, Takeharu Genes (Basel) Review 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. MDPI 2023-10-15 /pmc/articles/PMC10606877/ /pubmed/37895291 http://dx.doi.org/10.3390/genes14101942 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Terada, Nobuo Saitoh, Yurika Saito, Masaki Yamada, Tomoki Kamijo, Akio Yoshizawa, Takahiro Sakamoto, Takeharu Recent Progress on Genetically Modified Animal Models for Membrane Skeletal Proteins: The 4.1 and MPP Families |
title | Recent Progress on Genetically Modified Animal Models for Membrane Skeletal Proteins: The 4.1 and MPP Families |
title_full | Recent Progress on Genetically Modified Animal Models for Membrane Skeletal Proteins: The 4.1 and MPP Families |
title_fullStr | Recent Progress on Genetically Modified Animal Models for Membrane Skeletal Proteins: The 4.1 and MPP Families |
title_full_unstemmed | Recent Progress on Genetically Modified Animal Models for Membrane Skeletal Proteins: The 4.1 and MPP Families |
title_short | Recent Progress on Genetically Modified Animal Models for Membrane Skeletal Proteins: The 4.1 and MPP Families |
title_sort | recent progress on genetically modified animal models for membrane skeletal proteins: the 4.1 and mpp families |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10606877/ https://www.ncbi.nlm.nih.gov/pubmed/37895291 http://dx.doi.org/10.3390/genes14101942 |
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