GRAF1 forms a complex with MICAL-L1 and EHD1 to cooperate in tubular recycling endosome vesiculation

Bishuang Cai, Shuwei Xie, Steve Caplan, Naava Naslavsky

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


The biogenesis of tubular recycling endosomes (TREs) and their subsequent vesiculation after cargo-sorting has occurred, is essential for receptor and lipid recycling to the plasma membrane. Although recent studies have implicated the C-terminal Eps15 Homology Domain (EHD) protein, EHD1, as a key regulator of TRE vesiculation, additional proteins involved in this process have been largely uncharacterized. In the present study, we identify the GTPase Regulator Associated with Focal adhesion kinase-1 (GRAF1) protein in a complex with EHD1 and the TRE hub protein, Molecules Interacting with CasL-Like1 (MICAL-L1). Over-expression of GRAF1 caused vesiculation of MICAL-L1-containing TRE, whereas GRAF1-depletion led to impaired TRE vesiculation and delayed receptor recycling. Moreover, co-addition of purified EHD1 and GRAF1 in a semi-permeabilized cell vesiculation assay produced synergistic TRE vesiculation. Overall, based on our data, we suggest that in addition to its roles in clathrin-independent endocytosis, GRAF1 synergizes with EHD1 to support TRE vesiculation.

Original languageEnglish (US)
Article number22
JournalFrontiers in Cell and Developmental Biology
Issue numberMAY
StatePublished - May 27 2014


  • BAR domain
  • EHD1
  • GRAF1
  • MICAL-L1
  • PH domain
  • Tubular recycling endosome
  • Tubulation
  • Vesiculation

ASJC Scopus subject areas

  • Developmental Biology
  • Cell Biology


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