The cytosolic N-terminus of CD317/tetherin is a membrane microdomain exclusion motif.

Peter G. Billcliff, Oforiwa A. Gorleku, Luke Chamberlain, George Banting

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)
53 Downloads (Pure)


The integral membrane protein CD317/tetherin has been associated with a plethora of biological processes, including restriction of enveloped virus release, regulation of B cell growth, and organisation of membrane microdomains. CD317 possesses both a conventional transmembrane (TM) domain and a glycophosphatidylinositol (GPI) anchor. We confirm that the GPI anchor is essential for CD317 to associate with membrane microdomains, and that the TM domain of CD44 is unable to rescue proper microdomain association of a ΔGPI-CD317 construct. Additionally, we demonstrate that the cytosolic amino terminal region of CD317 can function as a 'microdomain-excluding' motif, when heterologously expressed as part of a reporter construct. Finally, we show that two recently described isoforms of CD317 do not differ in their affinity for membrane microdomains. Together, these data help further our understanding of the fundamental cell biology governing membrane microdomain association of CD317.
Original languageEnglish
Pages (from-to)1253-1263
Number of pages11
JournalOpen Biology
Issue number11
Early online date18 Oct 2013
Publication statusPublished - 15 Nov 2013


  • tetherin
  • membrane microdomain
  • lipid raft
  • palmitoylation


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