Abstract：
:Endoplasmic reticulum (ER) membrane contact sites (MCSs) mark positions where endosomes undergo fission for cargo sorting. To define the role of ER at this unique MCS, we targeted a promiscuous biotin ligase to cargo-sorting domains on endosome buds. This strategy identified the ER membrane protein TMCC1, a member of a conserved protein family. TMCC1 concentrates at the ER-endosome MCSs that are spatially and temporally linked to endosome fission. When TMCC1 is depleted, endosome morphology is normal, buds still form, but ER-associated bud fission and subsequent cargo sorting to the Golgi are impaired. We find that the endosome-localized actin regulator Coronin 1C is required for ER-associated fission of actin-dependent cargo-sorting domains. Coronin 1C is recruited to endosome buds independently of TMCC1, while TMCC1/ER recruitment requires Coronin 1C. This link between TMCC1 and Coronin 1C suggests that the timing of TMCC1-dependent ER recruitment is tightly regulated to occur after cargo has been properly sequestered into the bud.
journal_name
Celljournal_title
Cellauthors
Hoyer MJ,Chitwood PJ,Ebmeier CC,Striepen JF,Qi RZ,Old WM,Voeltz GKdoi
10.1016/j.cell.2018.08.030subject
Has Abstractpub_date
2018-09-20 00:00:00pages
254-265.e14issue
1eissn
0092-8674issn
1097-4172pii
S0092-8674(18)31046-8journal_volume
175pub_type
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