Abrogating ALIX Interactions Results in Stuttering of the ESCRT Machinery.
Abrogating ALIX Interactions Results in Stuttering of the ESCRT Machinery.
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DOI:
10.3390/v12091032
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发表时间:
2020-09-16
期刊:
影响因子:
--
通讯作者:
Saffarian S
中科院分区:
文献类型:
--
作者:
Gupta S;Bendjennat M;Saffarian S
Endosomal sorting complexes required for transport (ESCRT) proteins assemble on budding cellular membranes and catalyze their fission. Using live imaging of HIV virions budding from cells, we followed recruitment of ESCRT proteins ALIX, CHMP4B and VPS4. We report that the ESCRT proteins transiently co-localize with virions after completion of virion assembly for durations of 45 ± 30 s. We show that mutagenizing the YP domain of Gag which is the primary ALIX binding site or depleting ALIX from cells results in multiple recruitments of the full ESCRT machinery on the same virion (referred to as stuttering where the number of recruitments to the same virion >3). The stuttering recruitments are approximately 4 ± 3 min apart and have the same stoichiometry of ESCRTs and same residence time (45 ± 30 s) as the single recruitments in wild type interactions. Our observations suggest a role for ALIX during fission and question the linear model of ESCRT recruitment, suggesting instead a more complex co-assembly model.
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影响因子:
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作者:
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DOI:
10.1083/jcb.201110031
发表时间:
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期刊:
The Journal of cell biology
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