Structural determinants of REMORIN nanodomain formation in anionic membranes
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F23%3A00079828" target="_blank" >RIV/00159816:_____/23:00079828 - isvavai.cz</a>
Result on the web
<a href="https://www.sciencedirect.com/science/article/abs/pii/S0006349522039649" target="_blank" >https://www.sciencedirect.com/science/article/abs/pii/S0006349522039649</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bpj.2022.12.035" target="_blank" >10.1016/j.bpj.2022.12.035</a>
Alternative languages
Result language
angličtina
Original language name
Structural determinants of REMORIN nanodomain formation in anionic membranes
Original language description
Remorins are a family of multigenic plasma membrane phosphoproteins involved in biotic and abiotic plant inter-action mechanisms, partnering in molecular signaling cascades. Signaling activity of remorins depends on their phosphorylation states and subsequent clustering into nanosized membrane domains. The presence of a coiled-coil domain and a C-terminal domain is crucial to anchor remorins to negatively charged membrane domains; however, the exact role of the N-terminal intrinsically disordered domain (IDD) on protein clustering and lipid interactions is largely unknown. Here, we combine chemical biology and imaging approaches to study the partitioning of group 1 remorin into anionic model membranes mimicking the inner leaflet of the plant plasma membrane. Using reconstituted membranes containing a mix of saturated and unsaturated phosphatidylcholine, phosphatidylinositol phosphates, and sterol, we investigate the clustering of remorins to the membrane and monitor the formation of nanosized membrane domains. REM1.3 promoted membrane nanodomain organization on the exposed external leaflet of both spherical lipid vesicles and flat supported lipid bilayers. Our results reveal that REM1.3 drives a mechanism allowing lipid reorganization, leading to the formation of remorin-enriched nanodomains. Phosphorylation of the N-terminal IDD by the calcium protein kinase CPK3 influences this clustering and can lead to the formation of smaller and more disperse domains. Our work reveals the phosphate-dependent involvement of the N-terminal IDD in the remorin-mem-brane interaction process by driving structural rearrangements at lipid-water interfaces.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
BIOPHYSICAL JOURNAL
ISSN
0006-3495
e-ISSN
1542-0086
Volume of the periodical
122
Issue of the periodical within the volume
11
Country of publishing house
US - UNITED STATES
Number of pages
11
Pages from-to
2192-2202
UT code for WoS article
001016760400001
EID of the result in the Scopus database
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