Abstract:
:REMORINs are nanodomain-organized proteins located in the plasma membrane and involved in cellular responses in plants. The dynamic assembly of the membrane nanodomains represents an essential tool of the versatile membrane barriers to control and modulate cellular functions. Nevertheless, the assembly mechanisms and protein organization strategies of nanodomains are poorly understood and many structural aspects are difficult to visualize. Using an ensemble of biophysical approaches, including solid-state nuclear magnetic resonance, cryo-electron microscopy and in vivo confocal imaging, we provide first insights on the role and the structural mechanisms of REMORIN trimerization. Our results suggest that the formation of REMORIN coiled-coil trimers is essential for membrane recruitment and promotes REMORIN assembly in vitro into long filaments by trimer-trimer interactions that might participate in nanoclustering into membrane domains in vivo.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Martinez D,Legrand A,Gronnier J,Decossas M,Gouguet P,Lambert O,Berbon M,Verron L,Grélard A,Germain V,Loquet A,Mongrand S,Habenstein Bdoi
10.1016/j.jsb.2018.02.003subject
Has Abstractpub_date
2019-04-01 00:00:00pages
12-19issue
1eissn
1047-8477issn
1095-8657pii
S1047-8477(18)30046-7journal_volume
206pub_type
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