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Mechanistic insights into the interactions of NAP1 with the SKICH domains of NDP52 and TAX1BP1

Fu, Tao ; Liu, Jianping ; Wang, Yingli ; Xie, Xingqiao ; Hu, Shichen ; Pan, Lifeng

Proceedings of the National Academy of Sciences - PNAS, 2018-12, Vol.115 (50), p.E11651-E11660 [Periódico revisado por pares]

United States: National Academy of Sciences

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Mechanistic insights into the interactions of NAP1 with the SKICH domains of NDP52 and TAX1BP1
Autor: Fu, Tao ; Liu, Jianping ; Wang, Yingli ; Xie, Xingqiao ; Hu, Shichen ; Pan, Lifeng
Assuntos: Adaptor Proteins, Signal Transducing - chemistry ; Adaptor Proteins, Signal Transducing - genetics ; Adaptor Proteins, Signal Transducing - metabolism ; Amino Acid Sequence ; Autophagy ; Autophagy - physiology ; Binding ; Biological Sciences ; Crystallography, X-Ray ; Domains ; Green Fluorescent Proteins - chemistry ; Green Fluorescent Proteins - genetics ; Green Fluorescent Proteins - metabolism ; HeLa Cells ; Homology ; Humans ; Intracellular Signaling Peptides and Proteins - chemistry ; Intracellular Signaling Peptides and Proteins - genetics ; Intracellular Signaling Peptides and Proteins - metabolism ; Kinases ; Models, Molecular ; Neoplasm Proteins - chemistry ; Neoplasm Proteins - genetics ; Neoplasm Proteins - metabolism ; Nuclear Proteins - chemistry ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Phagocytosis ; Phosphorylation ; PNAS Plus ; Protein Interaction Domains and Motifs ; Protein Structure, Quaternary ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Proteins ; Proteins - chemistry ; Proteins - genetics ; Proteins - metabolism ; Receptors ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; Sequence Homology, Amino Acid ; tRNA Methyltransferases
É parte de: Proceedings of the National Academy of Sciences - PNAS, 2018-12, Vol.115 (50), p.E11651-E11660
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Author contributions: T.F., S.H., and L.P. designed research; T.F., Y.W., and X.X. performed research; T.F., J.L., X.X., and L.P. analyzed data; and T.F. and L.P. wrote the paper.
Edited by Beth Levine, The University of Texas Southwestern, Dallas, TX, and approved October 30, 2018 (received for review July 3, 2018)
Descrição: NDP52 and TAX1BP1, two SKIP carboxyl homology (SKICH) domain-containing autophagy receptors, play crucial roles in selective autophagy. The autophagic functions of NDP52 and TAX1BP1 are regulated by TANK-binding kinase 1 (TBK1), which may associate with them through the adaptor NAP1. However, the molecular mechanism governing the interactions of NAP1 with NDP52 and TAX1BP1, as well as the effects induced by TBK1-mediated phosphorylation of NDP52 and TAX1BP1, remains elusive. Here, we report the atomic structures of the SKICH regions of NDP52 and TAX1BP1 in complex with NAP1, which not only uncover the mechanistic bases underpinning the specific interactions of NAP1with the SKICH domains of NDP52 and TAX1BP1 but also reveal the binding mode of a SKICH domain. Moreover, we uncovered that the SKICH domains of NDP52 and TAX1BP1 share a general binding mode to interact with NAP1. Finally, we also evaluated the currently known TBK1-mediated phosphorylation sites in the SKICH domains of NDP52 and TAX1BP1 on the basis of their interactions with NAP1. In all, our findings provide mechanistic insights into the interactions of NAP1 with NDP52 and TAX1BP1, and are valuable for further understanding the functions of these proteins in selective autophagy.
Editor: United States: National Academy of Sciences
Idioma: Inglês

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Mechanistic insights into the interactions of NAP1 with the SKICH domains of NDP52 and TAX1BP1

Fu, Tao ; Liu, Jianping ; Wang, Yingli ; Xie, Xingqiao ; Hu, Shichen ; Pan, Lifeng

United States: National Academy of Sciences

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