A single β adaptin contributes to AP1 and AP2 complexes and clathrin function in Dictyostelium.

A single β adaptin contributes to AP1 and AP2 complexes and clathrin function in Dictyostelium.
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DOI:
10.1111/j.1600-0854.2011.01310.x
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发表时间:
2012-02
期刊:
Traffic (Copenhagen, Denmark)
影响因子:
--
通讯作者:
O'Halloran TJ
O'Halloran TJ
中科院分区:
其他
文献类型:
--
作者:
Sosa RT;Weber MM;Wen Y;O'Halloran TJ

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The assembly of clathrin-coated vesicles is important for numerous cellular processes, including nutrient uptake and membrane organization. Important contributors to clathrin assembly are four tetrameric Assembly Proteins, also called Adaptor Proteins (AP’s), each of which contains a beta subunit. We identified a single beta subunit, named β1/2, that contributes to both the AP1 and AP2 complexes of Dictyostelium. Disruption of the gene encoding β1/2 resulted in severe defects in growth, cytokinesis, and development. Additionally, cells lacking β1/2 displayed profound osmoregulatory defects including the absence of contractile vacuoles and mislocalization of contractile vacuole markers. The phenotypes of β1/2 were most similar to previously described phenotypes of clathrin and AP1 mutants, supporting a particularly important contribution of AP1 to clathrin pathways in Dictyostelium cells. The absence of β1/2 in cells led to significant reductions in the protein amounts of the medium-sized subunits of the AP1 and AP2 complexes, establishing a role for the beta subunit in the stability of the medium subunits. Dictyostelium β1/2 could resemble a common ancestor of the more specialized β1 and β2 subunits of the vertebrate AP complexes. Our results support the essential contribution a single beta subunit to the stability and function AP1 and AP2 in a simple eukaryote.
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