Glycosylation and lipids working in concert direct CD2 ectodomain orientation and presentation.
Proteins embedded in the plasma membrane mediate interactions with the cell environment and play decisive roles in many signaling events. For cell-cell recognition molecules it is highly likely that their structures and behavior have been optimized in ways that overcome the limitations of membrane t...
| Main Authors: | , , , , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
American Chemical Society
2017
|
| _version_ | 1797073673319874560 |
|---|---|
| author | Polley, A Orłowski, A Danne, R Gurtovenko, A Bernardino de la Serna, J Eggeling, C Davis, S Róg, T Vattulainen, I |
| author_facet | Polley, A Orłowski, A Danne, R Gurtovenko, A Bernardino de la Serna, J Eggeling, C Davis, S Róg, T Vattulainen, I |
| author_sort | Polley, A |
| collection | OXFORD |
| description | Proteins embedded in the plasma membrane mediate interactions with the cell environment and play decisive roles in many signaling events. For cell-cell recognition molecules it is highly likely that their structures and behavior have been optimized in ways that overcome the limitations of membrane tethering. In particular, the ligand binding regions of these proteins likely need to be maximally exposed. Here we show by means of atomistic simulations of membrane-bound CD2, a small cell adhesion receptor expressed by human T-cells and natural killer cells, that the presentation of its ectodomain is highly dependent on membrane lipids and receptor glycosylation acting in apparent unison. Detailed analysis shows that the underlying mechanism is based on electrostatic interactions complemented by steric interactions between glycans in the protein and the membrane surface. The findings are significant for understanding the factors that render membrane receptors accessible for binding and signaling. |
| first_indexed | 2024-03-06T23:25:26Z |
| format | Journal article |
| id | oxford-uuid:6a3492bc-d441-4ae6-88f0-5e27330eb0e4 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:25:26Z |
| publishDate | 2017 |
| publisher | American Chemical Society |
| record_format | dspace |
| spelling | oxford-uuid:6a3492bc-d441-4ae6-88f0-5e27330eb0e42022-03-26T18:55:57ZGlycosylation and lipids working in concert direct CD2 ectodomain orientation and presentation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6a3492bc-d441-4ae6-88f0-5e27330eb0e4EnglishSymplectic Elements at OxfordAmerican Chemical Society2017Polley, AOrłowski, ADanne, RGurtovenko, ABernardino de la Serna, JEggeling, CDavis, SRóg, TVattulainen, IProteins embedded in the plasma membrane mediate interactions with the cell environment and play decisive roles in many signaling events. For cell-cell recognition molecules it is highly likely that their structures and behavior have been optimized in ways that overcome the limitations of membrane tethering. In particular, the ligand binding regions of these proteins likely need to be maximally exposed. Here we show by means of atomistic simulations of membrane-bound CD2, a small cell adhesion receptor expressed by human T-cells and natural killer cells, that the presentation of its ectodomain is highly dependent on membrane lipids and receptor glycosylation acting in apparent unison. Detailed analysis shows that the underlying mechanism is based on electrostatic interactions complemented by steric interactions between glycans in the protein and the membrane surface. The findings are significant for understanding the factors that render membrane receptors accessible for binding and signaling. |
| spellingShingle | Polley, A Orłowski, A Danne, R Gurtovenko, A Bernardino de la Serna, J Eggeling, C Davis, S Róg, T Vattulainen, I Glycosylation and lipids working in concert direct CD2 ectodomain orientation and presentation. |
| title | Glycosylation and lipids working in concert direct CD2 ectodomain orientation and presentation. |
| title_full | Glycosylation and lipids working in concert direct CD2 ectodomain orientation and presentation. |
| title_fullStr | Glycosylation and lipids working in concert direct CD2 ectodomain orientation and presentation. |
| title_full_unstemmed | Glycosylation and lipids working in concert direct CD2 ectodomain orientation and presentation. |
| title_short | Glycosylation and lipids working in concert direct CD2 ectodomain orientation and presentation. |
| title_sort | glycosylation and lipids working in concert direct cd2 ectodomain orientation and presentation |
| work_keys_str_mv | AT polleya glycosylationandlipidsworkinginconcertdirectcd2ectodomainorientationandpresentation AT orłowskia glycosylationandlipidsworkinginconcertdirectcd2ectodomainorientationandpresentation AT danner glycosylationandlipidsworkinginconcertdirectcd2ectodomainorientationandpresentation AT gurtovenkoa glycosylationandlipidsworkinginconcertdirectcd2ectodomainorientationandpresentation AT bernardinodelasernaj glycosylationandlipidsworkinginconcertdirectcd2ectodomainorientationandpresentation AT eggelingc glycosylationandlipidsworkinginconcertdirectcd2ectodomainorientationandpresentation AT daviss glycosylationandlipidsworkinginconcertdirectcd2ectodomainorientationandpresentation AT rogt glycosylationandlipidsworkinginconcertdirectcd2ectodomainorientationandpresentation AT vattulaineni glycosylationandlipidsworkinginconcertdirectcd2ectodomainorientationandpresentation |