Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family

<table>Schematic representation of the domain organization of human arrestins and arrestin-domain containing (ARRDC) proteins, and yeast ARTs (arrestin-related trafficking adaptors). Domains detected by Pfam 26.0 (<a href="http://pfam.sanger.ac.uk/">http://pfam.sanger.ac.uk/</a>) are shown and correspond to the following Pfam-A accessions: Arr_N: PF00339, Arr_C: PF02752, Arr_N-like (Ldb19): PF13002, along with the corresponding E-values for each domain (NA: not applicable; ND: not detected; NS: not significant). A putative Arr_N domain in Ecm21/Art2 was identified by alignment with the presumed Arr_N domain of Csr2/Art8. Clathrin-binding sites are depicted on <svg height="13.425" id="M5" style="vertical-align:-2.29482pt" version="1.1" viewbox="0 0 8.8500004 13.425" width="8.8500004" xmlns="http://www.w3.org/2000/svg">
<g transform="matrix(1.25,0,0,-1.25,0,13.425)">
<g transform="translate(72,-61.26)">
<text transform="matrix(1,0,0,-1,-71.95,63.6)">
<tspan style="font-size: 12.50px; " x="0" y="0">𝛽</tspan>
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</g>
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</svg>-arrestins; potential binding sites for ubiquitin ligases of the Nedd4 family are also indicated on arrestin-related proteins.</table>

Biochemistry Research International

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Figure 1

Figure 1: Ubiquitin-Mediated Regulation of Endocytosis by Proteins of the Arrestin Family 