Seipin and the membrane-shaping protein Pex30 cooperate in organelle budding from the endoplasmic reticulum.

Seipin and the membrane-shaping protein Pex30 cooperate in organelle budding from the endoplasmic reticulum.
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DOI:
10.1038/s41467-018-05278-2
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发表时间:
2018-07-27
影响因子:
16.6
通讯作者:
Carvalho P
Carvalho P
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Wang S;Idrissi FZ;Hermansson M;Grippa A;Ejsing CS;Carvalho P

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脂滴和过氧化物酶体是真核细胞中普遍存在的重要细胞器。虽然这些细胞器的生物发生机制仍然难以捉摸,但两者似乎都需要内质网(ER)。在这里,我们表明,在酵母的ER出芽这些结构无关的细胞器有非常相似的要求,并涉及Pex30和seipin复杂之间的合作。在没有这些成分的情况下,LD和过氧化物酶体的出芽被抑制,导致其各自的组成分子,如三酰甘油和过氧化物酶体膜蛋白的ER积累,而COPII囊泡形成保持不受影响。这种表型可以通过重塑ER磷脂组成来逆转,突出了这些脂质在细胞器生物发生中的关键功能。我们建议,seipin和Pex30的行为一致,以组织允许细胞器出芽的膜域,并可能具有不同于散装ER的脂质组合物。脂滴(LDs)和过氧化物酶体都出现在内质网(ER)。在这里,作者表明,酵母Seipin和Pex30蛋白共同作用,以调节这些细胞器从ER的同一子域出芽。
Lipid droplets (LDs) and peroxisomes are ubiquitous organelles with central roles in eukaryotic cells. Although the mechanisms involved in biogenesis of these organelles remain elusive, both seem to require the endoplasmic reticulum (ER). Here we show that in yeast the ER budding of these structurally unrelated organelles has remarkably similar requirements and involves cooperation between Pex30 and the seipin complex. In the absence of these components, budding of both LDs and peroxisomes is inhibited, leading to the ER accumulation of their respective constituent molecules, such as triacylglycerols and peroxisomal membrane proteins, whereas COPII vesicle formation remains unaffected. This phenotype can be reversed by remodeling ER phospholipid composition highlighting a key function of these lipids in organelle biogenesis. We propose that seipin and Pex30 act in concert to organize membrane domains permissive for organelle budding, and that may have a lipid composition distinct from the bulk ER. Lipid droplets (LDs) and peroxisomes both emerge from the endoplasmic reticulum (ER). Here, the authors show that yeast Seipin and Pex30 proteins act together to regulate budding of these organelles from the same subdomain of the ER.
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