MAR1 links membrane adhesion to membrane merger during cell-cell fusion in Chlamydomonas.
MAR1 links membrane adhesion to membrane merger during cell-cell fusion in Chlamydomonas.
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DOI：
10.1016/j.devcel.2021.10.023
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发表时间：
2021-12-20
影响因子：
11.8
通讯作者：
Snell WJ
中科院分区：
文献类型：
--
作者：
Pinello JF;Liu Y;Snell WJ
Union of two gametes to form a zygote is a defining event in the life of sexual eukaryotes, yet the mechanisms that underlie cell-cell fusion during fertilization remain poorly characterized. Here, in studies of fertilization in the green alga, Chlamydomonas, we report identification of a membrane protein on minus gametes, Minus Adhesion Receptor 1 (MAR1), that is essential for the membrane attachment with plus gametes that immediately precedes lipid bilayer merger. We show that MAR1 forms a receptor pair with previously identified receptor FUS1 on plus gametes, whose ectodomain architecture we find is identical to a sperm adhesion protein conserved throughout plant lineages. Strikingly, before fusion, MAR1 is biochemically and functionally associated with the ancient, evolutionarily conserved eukaryotic class II fusion protein HAP2 on minus gametes. Thus, the integral membrane protein MAR1 provides a molecular link between membrane adhesion and bilayer merger during fertilization in Chlamydomonas. Gamete fusion in organisms across kingdoms depends on fusogen HAP2. Pinello et al. demonstrate that receptor MAR1 is associated with HAP2 on Chlamydomonas minus gametes and binds to conserved adhesion protein FUS1/GEX2 on plus gametes, suggesting a mechanism that ensures bilayer merger is triggered only upon lineage-specific gamete membrane attachment.
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