TY - JOUR
T1 - CED-6/GULP and components of the clathrin-mediated endocytosis machinery act redundantly to correctly display CED-1 on the cell membrane in Caenorhabditis elegans
AU - Harders, Rikke Hindsgaul
AU - Morthorst, Tine Hørning
AU - Landgrebe, Line
AU - Lande, Anna
AU - Sikjær Fuglsang, Marie
AU - Bothilde Mortensen, Stine
AU - Feteira Montero, Verónica
AU - Jensen, Helene Halkjær
AU - Wesseltoft, Jonas
AU - Olsen, Anders
N1 - © The Author(s) 2024. Published by Oxford University Press on behalf of The Genetics Society of America.
PY - 2024/7/8
Y1 - 2024/7/8
N2 - CED-1 (cell death abnormal) is a transmembrane receptor involved in the recognition of “eat-me” signals displayed on the surface of apoptotic cells and thus central for the subsequent engulfment of the cell corpse in Caenorhabditis elegans. The roles of CED-1 in engulfment are well established, as are its downstream effectors. The latter include the adapter protein CED-6/GULP and the ATP-binding cassette family homolog CED-7. However, how CED-1 is maintained on the plasma membrane in the absence of engulfment is currently unknown. Here, we show that CED-6 and CED-7 have a novel role in maintaining CED-1 correctly on the plasma membrane. We propose that the underlying mechanism is via endocytosis as CED-6 and CED-7 act redundantly with clathrin and its adaptor, the Adaptor protein 2 complex, in ensuring correct CED-1 localization. In conclusion, CED-6 and CED-7 impact other cellular processes than engulfment of apoptotic cells.
AB - CED-1 (cell death abnormal) is a transmembrane receptor involved in the recognition of “eat-me” signals displayed on the surface of apoptotic cells and thus central for the subsequent engulfment of the cell corpse in Caenorhabditis elegans. The roles of CED-1 in engulfment are well established, as are its downstream effectors. The latter include the adapter protein CED-6/GULP and the ATP-binding cassette family homolog CED-7. However, how CED-1 is maintained on the plasma membrane in the absence of engulfment is currently unknown. Here, we show that CED-6 and CED-7 have a novel role in maintaining CED-1 correctly on the plasma membrane. We propose that the underlying mechanism is via endocytosis as CED-6 and CED-7 act redundantly with clathrin and its adaptor, the Adaptor protein 2 complex, in ensuring correct CED-1 localization. In conclusion, CED-6 and CED-7 impact other cellular processes than engulfment of apoptotic cells.
KW - AP2
KW - CED-1
KW - CED-6/GULP
KW - CME
KW - Caenorhabditis elegans
KW - clathrin
KW - dynein
KW - endocytosis
UR - http://www.scopus.com/inward/record.url?scp=85197971094&partnerID=8YFLogxK
U2 - 10.1093/g3journal/jkae088
DO - 10.1093/g3journal/jkae088
M3 - Journal article
C2 - 38696649
SN - 2160-1836
VL - 14
JO - G3: Genes, Genomes, Genetics (Bethesda)
JF - G3: Genes, Genomes, Genetics (Bethesda)
IS - 7
M1 - jkae088
ER -