Knockdown analysis showed that interaction between MICALL1 and SYND2 was required for their localization to tubular REs, whereas EHD1 stabilized interaction between MICALL1 and SYND2 on recycling tubules. SYND2 colocalized with MICALL1 and EHD1 at tubular recycling endosomes (REs), with SYND2 and MICALL1 displaying similar dynamics of association with tubular membranes. (2013) demonstrated that the SH3 domain of SYND2 (SDC2 142460) interacted directly with 2 of the 14 proline-rich domains (PRDs) of MICALL1. Using immunoprecipitation analysis in HeLa cells, Giridharan et al. MICALL1 recruited and linked EHD1 and RAB8A ( 165040) on membrane tubules, thereby regulating endocytic recycling from the endocytic recycling compartment (ERC) to the plasma membrane. In contrast, MICALL1 was required for association of EHD1 with tubular membranes. However, association of MICALL1 with tubular membranes was independent of EHD1 and EHD3, as the C-terminal coiled-coli domain of MICALL1 alone was essential and sufficient for tubular localization. MICALL1 and EHD1 colocalized at tubular membranes in HeLa cells and were dynamically recruited to tubular membranes with similar kinetics. The interaction required the first NPF motif of MICALL1. Using pull-down, yeast 2-hybrid, and coimmunoprecipitation analyses, Sharma et al.
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