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Basolateral sorting of chloride channel 2 is mediated by interactions between a dileucine motif and the clathrin adaptor AP-1. | LitMetric

AI Article Synopsis

  • The mechanisms behind the subcellular localization of chloride channels, particularly ClC-2, remain largely unknown despite their crucial cellular functions.
  • ClC-2 is important for regulating cell volume and ion transport, and mutations affecting it lead to severe consequences like blindness and sterility in mice.
  • Recent studies identified ESMI(623)LL as a key signal for the basolateral sorting of ClC-2, highlighting the role of clathrin adaptors, both ubiquitous and epithelial-specific, in this process.

Article Abstract

In spite of the many key cellular functions of chloride channels, the mechanisms that mediate their subcellular localization are largely unknown. ClC-2 is a ubiquitous chloride channel usually localized to the basolateral domain of epithelia that regulates cell volume, ion transport, and acid-base balance; mice knocked out for ClC-2 are blind and sterile. Previous work suggested that CLC-2 is sorted basolaterally by TIFS(812)LL, a dileucine motif in CLC-2's C-terminal domain. However, our in silico modeling of ClC-2 suggested that this motif was buried within the channel's dimerization interface and identified two cytoplasmically exposed dileucine motifs, ESMI(623)LL and QVVA(635)LL, as candidate sorting signals. Alanine mutagenesis and trafficking assays support a scenario in which ESMI(623)LL acts as the authentic basolateral signal of ClC-2. Silencing experiments and yeast three-hybrid assays demonstrated that both ubiquitous (AP-1A) and epithelium-specific (AP-1B) forms of the tetrameric clathrin adaptor AP-1 are capable of carrying out basolateral sorting of ClC-2 through interactions of ESMI(623)LL with a highly conserved pocket in their γ1-σ1A hemicomplex.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4436783PMC
http://dx.doi.org/10.1091/mbc.E15-01-0047DOI Listing

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