Flippase-mediated phospholipid asymmetry promotes fast Cdc42 recycling in dynamic maintenance of cel...
Flippase-mediated phospholipid asymmetry promotes fast Cdc42 recycling in dynamic maintenance of cell polarity
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London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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In budding yeast, polarized Cdc42 localization is supported in part by guanine nucleotide dissociation inhibitor (GDI)-mediated extraction from the plasma membrane. Li and colleagues now show that a lipid flippase complex containing Lem3 and Dnf1 or Dnf2 contributes to membrane lipid asymmetry to facilitate GDI-mediated extraction of Cdc42.
Lipi...
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Full title
Flippase-mediated phospholipid asymmetry promotes fast Cdc42 recycling in dynamic maintenance of cell polarity
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3534761
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3534761
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ISSN
1465-7392
E-ISSN
1476-4679
DOI
10.1038/ncb2444
