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Structure paper

TitleTMEM16 scramblases thin the membrane to enable lipid scrambling.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 2604, Year 2022
Publish dateMay 11, 2022
AuthorsMaria E Falzone / Zhang Feng / Omar E Alvarenga / Yangang Pan / ByoungCheol Lee / Xiaolu Cheng / Eva Fortea / Simon Scheuring / Alessio Accardi /
PubMed AbstractTMEM16 scramblases dissipate the plasma membrane lipid asymmetry to activate multiple eukaryotic cellular pathways. Scrambling was proposed to occur with lipid headgroups moving between leaflets ...TMEM16 scramblases dissipate the plasma membrane lipid asymmetry to activate multiple eukaryotic cellular pathways. Scrambling was proposed to occur with lipid headgroups moving between leaflets through a membrane-spanning hydrophilic groove. Direct information on lipid-groove interactions is lacking. We report the 2.3 Å resolution cryogenic electron microscopy structure of the nanodisc-reconstituted Ca-bound afTMEM16 scramblase showing how rearrangement of individual lipids at the open pathway results in pronounced membrane thinning. Only the groove's intracellular vestibule contacts lipids, and mutagenesis suggests scrambling does not require specific protein-lipid interactions with the extracellular vestibule. We find scrambling can occur outside a closed groove in thinner membranes and is inhibited in thicker membranes, despite an open pathway. Our results show afTMEM16 thins the membrane to enable scrambling and that an open hydrophilic pathway is not a structural requirement to allow rapid transbilayer movement of lipids. This mechanism could be extended to other scramblases lacking a hydrophilic groove.
External linksNat Commun / PubMed:35562175 / PubMed Central
MethodsEM (single particle)
Resolution2.28 - 3.5 Å
Structure data

24717

7rwj

EMDB-24717, PDB-7rwj:
afTMEM16 in C22 lipid nanodiscs with MSP2N2 scaffold protein in the presnece of Ca2+
Method: EM (single particle) / Resolution: 3.5 Å

24722

7rx2

EMDB-24722, PDB-7rx2:
afTMEM16 in C22 lipid nanodiscs with MSP1E3 scaffold protein in the presnece of Ca2+
Method: EM (single particle) / Resolution: 2.7 Å

24723

7rx3

EMDB-24723, PDB-7rx3:
afTMEM16 in C14 lipid nanodiscs with MSP1E3 scaffold protein in the absence of Ca2+
Method: EM (single particle) / Resolution: 3.3 Å

24726

7rxa

EMDB-24726, PDB-7rxa:
afTMEM16 DE/AA mutant in C14 lipid nanodiscs in the presence of Ca2+
Method: EM (single particle) / Resolution: 3.08 Å

24727

7rxb

EMDB-24727, PDB-7rxb:
afTMEM16 lipid scramblase in C18 lipid nanodiscs in the absence of Ca2+
Method: EM (single particle) / Resolution: 3.07 Å

24730

7rxg

EMDB-24730, PDB-7rxg:
afTMEM16 in C18 lipid nanodiscs with MSP1E3 scaffold protein in the presence of Ca2+, full dimer
Method: EM (single particle) / Resolution: 2.28 Å

24731

7rxh

EMDB-24731, PDB-7rxh:
afTMEM16 in C18 lipid nanodiscs with MSP1E3 scaffold protein in the presence of Ca2+, monomer with extra lipids
Method: EM (single particle) / Resolution: 2.3 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-PGW:
(1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl / phospholipid*YM / Phosphatidylglycerol

ChemComp-HOH:
WATER / Water

Source
  • Aspergillus fumigatus (mold)
  • neosartorya fumigata (strain atcc mya-4609 / af293 / cbs 101355 / fgsc a1100) (mold)
  • neosartorya fumigata (strain cea10 / cbs 144.89 / fgsc a1163) (mold)
KeywordsLIPID TRANSPORT / TMEM16 / lipid scrambling

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