7yo9 | pdb_00007yo9
Crystal structure of fusion protein of human TP53INP2 LIR and human GABARAP
Structural highlights
FunctionGBRAP_HUMAN May play a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy (By similarity).[1] T53I2_HUMAN Dual regulator of transcription and autophagy. Positively regulates autophagy and is required for autophagosome formation and processing. May act as a scaffold protein that recruits MAP1LC3A, GABARAP and GABARAPL2 and brings them to the autophagosome membrane by interacting with VMP1 where, in cooperation with the BECN1-PI3-kinase class III complex, they trigger autophagosome development. Acts as a transcriptional activator of THRA.[2] [3] [4] Publication Abstract from PubMedABBREVIATIONS: A:C autophagic membrane:cytosol; ALS amyotrophic lateral sclerosis; ATG4 autophagy related 4; Atg8 autophagy related 8; BafA1 bafilomycin A1; BNIP3L/Nix BCL2 interacting protein 3 like; CALCOCO2/NDP52 calcium binding and coiled-coil domain 2; EBSS Earle's balanced salt solution; GABARAP GABA type A receptor-associated protein; GST glutathione S transferase; HKO hexa knockout; Kd dissociation constant; LIR LC3-interacting region; MAP1LC3/LC3 microtubule associated protein 1 light chain 3; NLS nuclear localization signal/sequence; PE phosphatidylethanolamine; SpHfl1 Schizosaccharomyces pombeorganic solute transmembrane transporter; SQSTM1/p62 SQSTM1/p62; TARDBP/TDP-43 TAR DNA binding protein; TKO triple knockout. Development of new tools to study membrane-anchored mammalian Atg8 proteins.,Park SW, Jeon P, Yamasaki A, Lee HE, Choi H, Mun JY, Jun YW, Park JH, Lee SH, Lee SK, Lee YK, Song HK, Lazarou M, Cho DH, Komatsu M, Noda NN, Jang DJ, Lee JA Autophagy. 2022 Oct 17:1-20. doi: 10.1080/15548627.2022.2132040. PMID:36250672[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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