%0 Generic %A J Klionsky, Daniel %A Popelka, Hana %D 2015 %T Analysis of the native conformation of the LIR/AIM motif in the Atg8/LC3/GABARAP-binding proteins %U https://tandf.figshare.com/articles/dataset/Analysis_of_the_native_conformation_of_the_LIR_AIM_motif_in_the_Atg8_LC3_GABARAP_binding_proteins/1601912 %R 10.6084/m9.figshare.1601912.v1 %2 https://ndownloader.figshare.com/files/2438990 %2 https://ndownloader.figshare.com/files/2438991 %2 https://ndownloader.figshare.com/files/2438992 %2 https://ndownloader.figshare.com/files/2438993 %K motif %K autophagy %K aim %K lir %K lc %K slim %K protein conformation %K binding partners %K atg %K consensus sequence %K region %X

The Atg8/LC3/GABARAP family of proteins, a group that has structural homology with ubiquitin, connects with a large set of binding partners to function in macroautophagy (hereafter autophagy). This interaction occurs primarily via a conserved motif termed the LC3-interacting region (LIR), or the Atg8-interacting motif (AIM). The consensus sequence for this motif, [W/F/Y]xx[L/I/V], can be found in many proteins, but only some of them are physiological partners containing a functional LIR/AIM. Because the structure of many full-length partners has not been, or cannot be, solved the structural context of the LIR/AIM within the native protein conformation is not obvious. Here we suggest that the functional LIR/AIM is a short linear motif (SLiM) protein-binding module, arising from an intrinsically disordered region. This finding enables the rapid elimination of some false Atg8/LC3/GABARAP-binding proteins, and connects the exponentially growing knowledge on disordered SLiMs with autophagy.

%I Taylor & Francis