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Domain architecture of selective autophagy cargo receptors known to date. Domain architecture of selective autophagy cargo receptors known to date. The.

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Presentation on theme: "Domain architecture of selective autophagy cargo receptors known to date. Domain architecture of selective autophagy cargo receptors known to date. The."— Presentation transcript:

1 Domain architecture of selective autophagy cargo receptors known to date.
Domain architecture of selective autophagy cargo receptors known to date. The sequestosome-1-like receptors (SLRs) constitute of p62, NBR1, NDP52, TAX1BP and OPTN (optineurin) in mammals. The known mitophagy receptors FUNDC1, BNIP3, NIX (BNIP3L) in mammals, and Atg32 in yeast, are shown. The specialized receptors Cbl and Stbd1, characterized in mammals, are involved in selective autophagy of Src kinase and glycogen, respectively. The Cvt cargo receptors, Atg19 and Atg34 in yeast, are essential for the Cvt pathway. PB1, Phox and Bem1 domain (dark pink); ZZ, ZZ-type zink finger domain (blue); CC, coiled-coil domain (light pink); NLS1 and NLS2, nuclear localization signals 1 and 2 (dark gray); NES, nuclear export signal (dark gray); LIR, LC3-interacting region (dark red); KIR, Keap interacting region (green); UBA, ubiquitin-associated domain (yellow); FW, four tryptophan domain (dark yellow); SKICH, SKIP carboxyl homology domain (light green); ZF, Zinc-finger domain (yellow); UBAN, ubiquitin binding in ABIN and NEMO domain (yellow); TM, transmembrane domain (light blue); BH3, Bcl-2 homology (BH) domain 3 (light purple); 4H, four-helix bundle domain (light gray); EF, EF-hand-fold domain (light gray); SH2, Src-homology 2 domain (light gray); Ring, really-interesting-new-gene-finger domain (blue); CBM20, family 20 carbohydrate-binding module domain (light gray); ABD, Ams1-binding domain (orange). The size of the receptors (in numbers of amino acids) is indicated. Åsa Birna Birgisdottir et al. J Cell Sci 2013;126: © Published by The Company of Biologists Ltd


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