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@ARTICLE{MacarrnPalacios:299563,
      author       = {V. Macarrón-Palacios and J. Hubrich and M. A. do Rego
                      Barros Fernandes Lima and N. G. Metzendorf and S. Kneilmann
                      and M. Trapp$^*$ and C. Acuna and A. Patrizi$^*$ and E.
                      D'Este and M. W. Kilimann},
      title        = {{P}aralemmin-1 controls the nanoarchitecture of the
                      neuronal submembrane cytoskeleton.},
      journal      = {Science advances},
      volume       = {11},
      number       = {10},
      issn         = {2375-2548},
      address      = {Washington, DC [u.a.]},
      publisher    = {Assoc.},
      reportid     = {DKFZ-2025-00504},
      pages        = {eadt3724},
      year         = {2025},
      note         = {DKFZ-ZMBH Alliance},
      abstract     = {The submembrane cytoskeleton of neurons displays a highly
                      ordered 190-nanometer periodic actin-spectrin lattice, the
                      membrane-associated periodic skeleton (MPS). It is involved
                      in mechanical resilience, signaling, and action potential
                      transmission. Here, we identify paralemmin-1 (Palm1) as a
                      component and regulator of the MPS. Palm1 binds to the
                      amino-terminal region of βII-spectrin, and MINFLUX
                      microscopy localizes it in close proximity (<20 nanometers)
                      to the actin-capping protein and MPS component adducin.
                      Combining overexpression, knockout, and rescue experiments,
                      we observe that the expression level of Palm1 controls the
                      degree of periodicity of the MPS and also affects the
                      electrophysiological properties of neurons. A single amino
                      acid mutation (W54A) in Palm1 abolishes the MPS binding and
                      remodeling activities of Palm1. Our findings identify Palm1
                      as a protein specifically dedicated to organizing the MPS
                      and will advance the understanding of the assembly and
                      plasticity of the actin-spectrin submembrane skeleton in
                      general.},
      keywords     = {Neurons: metabolism / Neurons: cytology / Cytoskeleton:
                      metabolism / Animals / Protein Binding / Humans / Spectrin:
                      metabolism / Spectrin: genetics / Actins: metabolism / Cell
                      Membrane: metabolism / Cytoskeletal Proteins: metabolism /
                      Cytoskeletal Proteins: genetics / Mice / Spectrin (NLM
                      Chemicals) / Actins (NLM Chemicals) / Cytoskeletal Proteins
                      (NLM Chemicals)},
      cin          = {A320},
      ddc          = {500},
      cid          = {I:(DE-He78)A320-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40053592},
      pmc          = {pmc:PMC11887803},
      doi          = {10.1126/sciadv.adt3724},
      url          = {https://inrepo02.dkfz.de/record/299563},
}