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@ARTICLE{Pinotsis:454500,
      author       = {Pinotsis, Nikos and Zielinska, Karolina and Babuta, Mrigya
                      and Arolas, Joan L. and Kostan, Julius and Khan, Muhammad
                      Bashir and Schreiner, Claudia and Salmazo, Anita and
                      Ciccarelli, Luciano and Puchinger, Martin and Gkougkoulia,
                      Eirini A. and Ribeiro, Euripedes de Almeida and Marlovits,
                      Thomas and Bhattacharya, Alok and Djinovic-Carugo, Kristina},
      title        = {{C}alcium modulates the domain flexibility and function of
                      an $\alpha$-actinin similar to the ancestral α-actinin},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {117},
      number       = {36},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {PUBDB-2021-00574},
      pages        = {22101 - 22112},
      year         = {2020},
      note         = {Waiting for fulltext},
      abstract     = {The actin cytoskeleton, a dynamic network of actin
                      filaments and associated F-actin–binding proteins, is
                      fundamentally important in eukaryotes. α-Actinins are major
                      F-actin bundlers that are inhibited by Ca$^{2+}$ in
                      nonmuscle cells. Here we report the mechanism of
                      Ca$^{2+}$-mediated regulation of Entamoeba histolytica
                      α-actinin-2 (EhActn2) with features expected for the common
                      ancestor of Entamoeba and higher eukaryotic α-actinins.
                      Crystal structures of Ca$^{2+}$-free and Ca$^{2+}$-bound
                      EhActn2 reveal a calmodulin-like domain (CaMD) uniquely
                      inserted within the rod domain. Integrative studies reveal
                      an exceptionally high affinity of the EhActn2 CaMD for
                      Ca$^{2+}$, binding of which can only be regulated in the
                      presence of physiological concentrations of Mg$^{2+}$.
                      C$^{2+}$ binding triggers an increase in protein multidomain
                      rigidity, reducing conformational flexibility of
                      F-actin–binding domains via interdomain cross-talk and
                      consequently inhibiting F-actin bundling. In vivo studies
                      uncover that EhActn2 plays an important role in phagocytic
                      cup formation and might constitute a new drug target for
                      amoebic dysentery.},
      cin          = {CSSB-UKE / CSSB-GS / CSSB-UKE-TM},
      ddc          = {500},
      cid          = {I:(DE-H253)CSSB-UKE-20141216 / I:(DE-H253)CSSB-GS-20140311
                      / I:(DE-H253)CSSB-UKE-TM-20210520},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32848067},
      UT           = {WOS:000572964500012},
      doi          = {10.1073/pnas.1917269117},
      url          = {https://bib-pubdb1.desy.de/record/454500},
}