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- W2891870105 abstract "Arrestins are key adaptor proteins that control the fate of cell-surface membrane proteins and modulate downstream signaling cascades. Dictyostelium discoideum genome encodes six arrestin-related proteins, harboring additional modules besides the arrestin domain. Here, we studied AdcB and AdcC, two homologs that contain C2 and SAM-domains. We showed that AdcC, in contrast to AdcB, responds to various stimuli (such as the chemoattractants cAMP and folate) known to induce a cytosolic calcium rise by a transient translocation to the plasma membrane and that calcium is a direct regulator of AdcC localization. This response requires the calcium-dependent membrane targeting C2 domain and the double SAM domain involved in AdcC oligomerization, revealing a mode of membrane targeting and regulation unique among members of the arrestin clan. AdcB shares several biochemical properties with AdcC including in vitro binding to anionic lipids in a calcium-dependent manner and auto-assembly as large homo-oligomers. AdcB can interact with AdcC; still its intracellular localization is insensitive to calcium. Despite their high degree of homology and common characteristics, AdcB and AdcC are therefore likely to fulfill distinct functions in amoeba." @default.
- W2891870105 created "2018-09-27" @default.
- W2891870105 creator A5059167576 @default.
- W2891870105 creator A5065895522 @default.
- W2891870105 creator A5079819128 @default.
- W2891870105 creator A5081442476 @default.
- W2891870105 creator A5088044963 @default.
- W2891870105 date "2018-01-01" @default.
- W2891870105 modified "2023-10-15" @default.
- W2891870105 title "Calcium influx mediates the chemoattractant-induced translocation of the arrestin-related protein AdcC in <i>Dictyostelium</i>" @default.
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- W2891870105 doi "https://doi.org/10.1242/jcs.207951" @default.
- W2891870105 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30209138" @default.
- W2891870105 hasPublicationYear "2018" @default.
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