MPP1 Determines the Mobility of Flotillins and Controls the Confinement of Raft-Associated Molecules
MPP1 (membrane palmitoylated protein 1) belongs to the MAGUK (membrane-associated guanylate kinase homologs) scaffolding protein family. These proteins organize molecules into complexes, thereby maintaining the structural heterogeneity of the plasma membrane (PM). Our previous results indicated that...
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MDPI AG
2022-01-01
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| Online Access: | https://www.mdpi.com/2073-4409/11/3/311 |
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| author | Agnieszka Biernatowska Karolina Wójtowicz Tomasz Trombik Aleksander F. Sikorski Aleksander Czogalla |
| author_facet | Agnieszka Biernatowska Karolina Wójtowicz Tomasz Trombik Aleksander F. Sikorski Aleksander Czogalla |
| author_sort | Agnieszka Biernatowska |
| collection | DOAJ |
| description | MPP1 (membrane palmitoylated protein 1) belongs to the MAGUK (membrane-associated guanylate kinase homologs) scaffolding protein family. These proteins organize molecules into complexes, thereby maintaining the structural heterogeneity of the plasma membrane (PM). Our previous results indicated that direct, high-affinity interactions between MPP1 and flotillins (raft marker proteins) display dominant PM-modulating capacity in erythroid cells. In this study, with high-resolution structured illuminated imaging, we investigated how these complexes are organized within erythroid cells on the nanometer scale. Furthermore, using other spectroscopic techniques, namely fluorescence recovery after photobleaching (FRAP) and spot-variation fluorescence correlation spectroscopy (svFCS), we revealed that MPP1 acts as a key raft-capturing molecule, regulating temporal immobilization of flotillin-based nanoclusters, and controls local concentration and confinement of sphingomyelin and Thy-1 in raft nanodomains. Our data enabled us to uncover molecular principles governing the key involvement of MPP1-flotillin complexes in the dynamic nanoscale organization of PM of erythroid cells. |
| first_indexed | 2024-03-10T00:05:37Z |
| format | Article |
| id | doaj.art-ba71fbca036d407d9aaab0b3f9f98f41 |
| institution | Directory Open Access Journal |
| issn | 2073-4409 |
| language | English |
| last_indexed | 2024-03-10T00:05:37Z |
| publishDate | 2022-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Cells |
| spelling | doaj.art-ba71fbca036d407d9aaab0b3f9f98f412023-11-23T16:09:46ZengMDPI AGCells2073-44092022-01-0111331110.3390/cells11030311MPP1 Determines the Mobility of Flotillins and Controls the Confinement of Raft-Associated MoleculesAgnieszka Biernatowska0Karolina Wójtowicz1Tomasz Trombik2Aleksander F. Sikorski3Aleksander Czogalla4Department of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, ul. F. Joliot-Curie 14a, 50-383 Wrocław, PolandDepartment of Biotransformation, Faculty of Biotechnology, University of Wrocław, ul. F. Joliot-Curie 14a, 50-383 Wrocław, PolandDepartment of Biophysics, Faculty of Biotechnology, University of Wrocław, ul. F. Joliot-Curie 14a, 50-383 Wrocław, PolandResearch and Development Center, Regional Specialist Hospital, Kamieńskiego 73a, 51-154 Wrocław, PolandDepartment of Cytobiochemistry, Faculty of Biotechnology, University of Wrocław, ul. F. Joliot-Curie 14a, 50-383 Wrocław, PolandMPP1 (membrane palmitoylated protein 1) belongs to the MAGUK (membrane-associated guanylate kinase homologs) scaffolding protein family. These proteins organize molecules into complexes, thereby maintaining the structural heterogeneity of the plasma membrane (PM). Our previous results indicated that direct, high-affinity interactions between MPP1 and flotillins (raft marker proteins) display dominant PM-modulating capacity in erythroid cells. In this study, with high-resolution structured illuminated imaging, we investigated how these complexes are organized within erythroid cells on the nanometer scale. Furthermore, using other spectroscopic techniques, namely fluorescence recovery after photobleaching (FRAP) and spot-variation fluorescence correlation spectroscopy (svFCS), we revealed that MPP1 acts as a key raft-capturing molecule, regulating temporal immobilization of flotillin-based nanoclusters, and controls local concentration and confinement of sphingomyelin and Thy-1 in raft nanodomains. Our data enabled us to uncover molecular principles governing the key involvement of MPP1-flotillin complexes in the dynamic nanoscale organization of PM of erythroid cells.https://www.mdpi.com/2073-4409/11/3/311MPP1flotillinsraft nanodomains |
| spellingShingle | Agnieszka Biernatowska Karolina Wójtowicz Tomasz Trombik Aleksander F. Sikorski Aleksander Czogalla MPP1 Determines the Mobility of Flotillins and Controls the Confinement of Raft-Associated Molecules Cells MPP1 flotillins raft nanodomains |
| title | MPP1 Determines the Mobility of Flotillins and Controls the Confinement of Raft-Associated Molecules |
| title_full | MPP1 Determines the Mobility of Flotillins and Controls the Confinement of Raft-Associated Molecules |
| title_fullStr | MPP1 Determines the Mobility of Flotillins and Controls the Confinement of Raft-Associated Molecules |
| title_full_unstemmed | MPP1 Determines the Mobility of Flotillins and Controls the Confinement of Raft-Associated Molecules |
| title_short | MPP1 Determines the Mobility of Flotillins and Controls the Confinement of Raft-Associated Molecules |
| title_sort | mpp1 determines the mobility of flotillins and controls the confinement of raft associated molecules |
| topic | MPP1 flotillins raft nanodomains |
| url | https://www.mdpi.com/2073-4409/11/3/311 |
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