Nanodomain remorin oligomerization status fine-tunes formin activity in actin nucleation
Nanodomains are nanometer scale subcompartments in dynamic plasma membrane, enriched in specific lipids and protein components that manage cellular processes. A well-characterized marker for lipid nanodomain, remorin protein has been identified in involving nanodomain clustering. The assembly of nan...
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| Format: | Final Year Project (FYP) |
| Language: | English |
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Nanyang Technological University
2022
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| Online Access: | https://hdl.handle.net/10356/157112 |
| _version_ | 1811676483587932160 |
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| author | Sim, Jia Xin |
| author2 | Miao Yansong |
| author_facet | Miao Yansong Sim, Jia Xin |
| author_sort | Sim, Jia Xin |
| collection | NTU |
| description | Nanodomains are nanometer scale subcompartments in dynamic plasma membrane, enriched in specific lipids and protein components that manage cellular processes. A well-characterized marker for lipid nanodomain, remorin protein has been identified in involving nanodomain clustering. The assembly of nanodomain remorin and actin nucleating formin protein at cell surface act functional roles in promoting actin cytoskeleton polymerization during plant innate response. The biochemical activity of remorin is mostly controlled by N-terminal intrinsically disordered region (IDR), coiled-coil (CC) domain, and C-terminal membrane anchoring region, but less is known about the specificity driven by protein multivalency. Herein, we design multivalent recombinant remorin proteins with different CC oligomerization status and determine the underlying association of remorin oligomerization with formin nucleating protein. Due to multivalent cooperativity, remorin oligomers show self-assembly upon binding on membrane surface. In bulk pyrene actin assay, formin positively regulates actin polymerization, either directly or as mediated by remorin oligomers. This indicates that the degree of remorin oligomerization influences formin to nucleate actin. Furthermore, remorin with trimeric coiled-coil structure is likely to facilitate membrane anchoring and formin-dependent actin polymerization, while a potent inhibition of actin nucleation is detected when guided by higher-order remorin oligomers. Such nanodomain remorin mediated regulation of formin is expected to fine-tune immune signals transduction in plant host. |
| first_indexed | 2024-10-01T02:22:12Z |
| format | Final Year Project (FYP) |
| id | ntu-10356/157112 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T02:22:12Z |
| publishDate | 2022 |
| publisher | Nanyang Technological University |
| record_format | dspace |
| spelling | ntu-10356/1571122023-02-28T18:09:40Z Nanodomain remorin oligomerization status fine-tunes formin activity in actin nucleation Sim, Jia Xin Miao Yansong School of Biological Sciences yansongm@ntu.edu.sg Science::Biological sciences Nanodomains are nanometer scale subcompartments in dynamic plasma membrane, enriched in specific lipids and protein components that manage cellular processes. A well-characterized marker for lipid nanodomain, remorin protein has been identified in involving nanodomain clustering. The assembly of nanodomain remorin and actin nucleating formin protein at cell surface act functional roles in promoting actin cytoskeleton polymerization during plant innate response. The biochemical activity of remorin is mostly controlled by N-terminal intrinsically disordered region (IDR), coiled-coil (CC) domain, and C-terminal membrane anchoring region, but less is known about the specificity driven by protein multivalency. Herein, we design multivalent recombinant remorin proteins with different CC oligomerization status and determine the underlying association of remorin oligomerization with formin nucleating protein. Due to multivalent cooperativity, remorin oligomers show self-assembly upon binding on membrane surface. In bulk pyrene actin assay, formin positively regulates actin polymerization, either directly or as mediated by remorin oligomers. This indicates that the degree of remorin oligomerization influences formin to nucleate actin. Furthermore, remorin with trimeric coiled-coil structure is likely to facilitate membrane anchoring and formin-dependent actin polymerization, while a potent inhibition of actin nucleation is detected when guided by higher-order remorin oligomers. Such nanodomain remorin mediated regulation of formin is expected to fine-tune immune signals transduction in plant host. Bachelor of Science in Biological Sciences 2022-05-08T23:48:52Z 2022-05-08T23:48:52Z 2022 Final Year Project (FYP) Sim, J. X. (2022). Nanodomain remorin oligomerization status fine-tunes formin activity in actin nucleation. Final Year Project (FYP), Nanyang Technological University, Singapore. https://hdl.handle.net/10356/157112 https://hdl.handle.net/10356/157112 en application/pdf Nanyang Technological University |
| spellingShingle | Science::Biological sciences Sim, Jia Xin Nanodomain remorin oligomerization status fine-tunes formin activity in actin nucleation |
| title | Nanodomain remorin oligomerization status fine-tunes formin activity in actin nucleation |
| title_full | Nanodomain remorin oligomerization status fine-tunes formin activity in actin nucleation |
| title_fullStr | Nanodomain remorin oligomerization status fine-tunes formin activity in actin nucleation |
| title_full_unstemmed | Nanodomain remorin oligomerization status fine-tunes formin activity in actin nucleation |
| title_short | Nanodomain remorin oligomerization status fine-tunes formin activity in actin nucleation |
| title_sort | nanodomain remorin oligomerization status fine tunes formin activity in actin nucleation |
| topic | Science::Biological sciences |
| url | https://hdl.handle.net/10356/157112 |
| work_keys_str_mv | AT simjiaxin nanodomainremorinoligomerizationstatusfinetunesforminactivityinactinnucleation |