The myelin proteolipid plasmolipin forms oligomers and induces liquid-ordered membranes in the Golgi complex

Yakey Yaffe, Ilan Hugger, Inbar Nevo Yassaf, Jeanne Shepshelovitch, Ella H. Sklan, Yechiel Elkabetz, Adva Yeheskel, Metsada Pasmanik-Chor, Carola Benzing, Alexander Macmillan, Katharina Gaus, Yael Eshed-Eisenbach, Elior Peles, Koret Hirschberg

Research output: Contribution to journalArticlepeer-review


Myelin comprises a compactly stacked massive surface area of protein-poor thick membrane that insulates axons to allow fast signal propagation. Increasing levels of themyelin protein plasmolipin (PLLP) were correlated with post-natal myelination; however, its function is unknown. Here, the intracellular localization and dynamics of PLLP were characterized in primary glial and cultured cells using fluorescently labeled PLLP and antibodies against PLLP. PLLP localized to and recycled between the plasma membrane and the Golgi complex. In the Golgi complex, PLLP forms oligomers based on fluorescence resonance energy transfer (FRET) analyses. PLLP oligomers blocked Golgi to plasma membrane transport of the secretory protein vesicular stomatitis virus G protein (VSVG), but not of a VSVGmutant with an elongated transmembrane domain. Laurdan staining analysis showed that this block is associated with PLLP-induced proliferation of liquid-ordered membranes. These findings show the capacity of PLLP to assemble potential myelin membrane precursor domains at the Golgi complex through its oligomerization and ability to attract liquid-ordered lipids. These data support amodel in which PLLP functions in myelin biogenesis through organization of myelin liquid-ordered membranes in the Golgi complex.

Original languageEnglish
Pages (from-to)2293-2302
Number of pages10
JournalJournal of Cell Science
Issue number13
StatePublished - 2015


  • Golgi complex
  • Myelin
  • Plasmolipin


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