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@ARTICLE{Krichel:872750,
      author       = {Krichel, Carsten and Möckel, Christina and Schillinger,
                      Oliver and Huesgen, Pitter F. and Sticht, Heinrich and
                      Strodel, Birgit and Weiergräber, Oliver H. and Willbold,
                      Dieter and Neudecker, Philipp},
      title        = {{S}olution structure of the autophagy-related protein
                      {LC}3{C} reveals a polyproline {II} motif on a mobile tether
                      with phosphorylation site},
      journal      = {Scientific reports},
      volume       = {9},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {FZJ-2020-00228},
      pages        = {14167},
      year         = {2019},
      abstract     = {(Macro-)autophagy is a compartmental degradation pathway
                      conserved from yeast to mammals. The yeast protein Atg8
                      mediates membrane tethering/hemifusion and cargo recruitment
                      and is essential for autophagy. The human MAP1LC3/GABARAP
                      family proteins show high sequence identity with Atg8, but
                      MAP1LC3C is distinguished by a conspicuous amino-terminal
                      extension with unknown functional significance. We have
                      determined the high-resolution three-dimensional structure
                      and measured the backbone dynamics of MAP1LC3C by NMR
                      spectroscopy. From Ser18 to Ala120, MAP1LC3C forms an
                      α-helix followed by the ubiquitin-like tertiary fold with
                      two hydrophobic binding pockets used by MAP1LC3/GABARAP
                      proteins to recognize targets presenting LC3-interacting
                      regions (LIRs). Unlike other MAP1LC3/GABARAP proteins, the
                      amino-terminal region of MAP1LC3C does not form a stable
                      helix α1 but a “sticky arm” consisting of a polyproline
                      II motif on a flexible linker. Ser18 at the interface
                      between this linker and the structural core can be
                      phosphorylated in vitro by protein kinase A, which causes
                      additional conformational heterogeneity as monitored by NMR
                      spectroscopy and molecular dynamics simulations, including
                      changes in the LIR-binding interface. Based on these results
                      we propose that the amino-terminal polyproline II motif
                      mediates specific interactions with the microtubule
                      cytoskeleton and that Ser18 phosphorylation modulates the
                      interplay of MAP1LC3C with its various target proteins.},
      cin          = {ICS-6 / ZEA-3},
      ddc          = {600},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / I:(DE-Juel1)ZEA-3-20090406},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31578424},
      UT           = {WOS:000488481500030},
      doi          = {10.1038/s41598-019-48155-8},
      url          = {https://juser.fz-juelich.de/record/872750},
}