% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Gregorczyk:276083,
      author       = {M. Gregorczyk and G. Pastore and I. Muñoz and T. Carroll
                      and J. Streubel$^*$ and M. Munro and P. Lis and S. Lange and
                      F. Lamoliatte and T. Macartney and R. Toth and F. Brown and
                      J. Hastie and G. Pereira$^*$ and D. Durocher and J. Rouse},
      title        = {{F}unctional characterization of {C}21{ORF}2 association
                      with the {NEK}1 kinase mutated in human in diseases.},
      journal      = {Life science alliance},
      volume       = {6},
      number       = {7},
      issn         = {2575-1077},
      address      = {Heidelberg},
      publisher    = {EMBO Press},
      reportid     = {DKFZ-2023-00989},
      pages        = {e202201740 -},
      year         = {2023},
      note         = {DKFZ-ZMBH Alliance},
      abstract     = {The NEK1 kinase controls ciliogenesis, mitosis, and DNA
                      repair, and NEK1 mutations cause human diseases including
                      axial spondylometaphyseal dysplasia and amyotrophic lateral
                      sclerosis. C21ORF2 mutations cause a similar pattern of
                      human diseases, suggesting close functional links with NEK1
                      Here, we report that endogenous NEK1 and C21ORF2 form a
                      tight complex in human cells. A C21ORF2 interaction domain
                      'CID' at the C-terminus of NEK1 is necessary for its
                      association with C21ORF2 in cells, and pathogenic mutations
                      in this region disrupt the complex. AlphaFold modelling
                      predicts an extended binding interface between a
                      leucine-rich repeat domain in C21ORF2 and the NEK1-CID, and
                      our model may explain why pathogenic mutations perturb the
                      complex. We show that NEK1 mutations that inhibit kinase
                      activity or weaken its association with C21ORF2 severely
                      compromise ciliogenesis, and that C21ORF2, like NEK1 is
                      required for homologous recombination. These data enhance
                      our understanding of how the NEK1 kinase is regulated, and
                      they shed light on NEK1-C21ORF2-associated diseases.},
      keywords     = {Humans / NIMA-Related Kinase 1: genetics / Mutation:
                      genetics / DNA Repair / Osteochondrodysplasias: genetics /
                      Phosphorylation / NIMA-Related Kinase 1 (NLM Chemicals) /
                      NEK1 protein, human (NLM Chemicals)},
      cin          = {A180},
      ddc          = {570},
      cid          = {I:(DE-He78)A180-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37188479},
      pmc          = {pmc:PMC10185812},
      doi          = {10.26508/lsa.202201740},
      url          = {https://inrepo02.dkfz.de/record/276083},
}