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@ARTICLE{GimnezMascarell:276852,
      author       = {Giménez-Mascarell, Paula and Oyenarte, Iker and Hardy,
                      Serge and Breiderhoff, Tilman and Stuiver, Marchel and
                      Kostantin, Elie and Diercks, Tammo and Pey, Angel L and
                      Ereño-Orbea, June and Martínez-Chantar, María Luz and
                      Khalaf-Nazzal, Reham and Claverie-Martin, Felix and Müller,
                      Dominik and Tremblay, Michel L and Martínez-Cruz, Luis
                      Alfonso},
      title        = {{S}tructural {B}asis of the {O}ncogenic {I}nteraction of
                      {P}hosphatase {PRL}-1 with the {M}agnesium {T}ransporter
                      {CNNM}2.},
      journal      = {JBC papers in press},
      volume       = {292},
      number       = {3},
      issn         = {0021-9258},
      address      = {Bethesda, MD},
      publisher    = {American Soc. for Biochemistry and Molecular Biology},
      reportid     = {DZNE-2025-00365},
      pages        = {786 - 801},
      year         = {2017},
      note         = {ISSN 0021-9258 not unique: **2 hits**.},
      abstract     = {Phosphatases of regenerating liver (PRLs), the most
                      oncogenic of all protein-tyrosine phosphatases (PTPs), play
                      a critical role in metastatic progression of cancers. Recent
                      findings established a new paradigm by uncovering that their
                      association with magnesium transporters of the cyclin M
                      (CNNM) family causes a rise in intracellular magnesium
                      levels that promote oncogenic transformation. Recently,
                      however, essential roles for regulation of the circadian
                      rhythm and reproduction of the CNNM family have been
                      highlighted. Here, we describe the crystal structure of
                      PRL-1 in complex with the Bateman module of CNNM2
                      (CNNM2BAT), which consists of two cystathionine β-synthase
                      (CBS) domains (IPR000664) and represents an intracellular
                      regulatory module of the transporter. The structure reveals
                      a heterotetrameric association, consisting of a disc-like
                      homodimer of CNNM2BAT bound to two independent PRL-1
                      molecules, each one located at opposite tips of the disc.
                      The structure highlights the key role played by Asp-558 at
                      the extended loop of the CBS2 motif of CNNM2 in maintaining
                      the association between the two proteins and proves that the
                      interaction between CNNM2 and PRL-1 occurs via the catalytic
                      domain of the phosphatase. Our data shed new light on the
                      structural basis underlying the interaction between PRL
                      phosphatases and CNNM transporters and provides a hypothesis
                      about the molecular mechanism by which PRL-1, upon binding
                      to CNNM2, might increase the intracellular concentration of
                      Mg2+ thereby contributing to tumor progression and
                      metastasis. The availability of this structure sets the
                      basis for the rational design of compounds modulating PRL-1
                      and CNNM2 activities.},
      keywords     = {Animals / Cation Transport Proteins: chemistry / Cation
                      Transport Proteins: genetics / Cation Transport Proteins:
                      metabolism / Immediate-Early Proteins: chemistry /
                      Immediate-Early Proteins: genetics / Immediate-Early
                      Proteins: metabolism / Magnesium: chemistry / Magnesium:
                      metabolism / Mice / Neoplasm Metastasis / Neoplasms:
                      genetics / Neoplasms: metabolism / Neoplasms: pathology /
                      Oncogene Proteins: chemistry / Oncogene Proteins: genetics /
                      Oncogene Proteins: metabolism / Protein Binding / Protein
                      Domains / Protein Structure, Secondary / Protein Tyrosine
                      Phosphatases: chemistry / Protein Tyrosine Phosphatases:
                      genetics / Protein Tyrosine Phosphatases: metabolism /
                      PRL-1, CNNM2, CBS domain (Other) / cancer (Other) / cell
                      proliferation (Other) / magnesium (Other) / phosphatase
                      (Other) / transporter (Other) / Cation Transport Proteins
                      (NLM Chemicals) / Cnnm2 protein, mouse (NLM Chemicals) /
                      Immediate-Early Proteins (NLM Chemicals) / Oncogene Proteins
                      (NLM Chemicals) / Protein Tyrosine Phosphatases (NLM
                      Chemicals) / Ptp4a1 protein, mouse (NLM Chemicals) /
                      Magnesium (NLM Chemicals)},
      ddc          = {610},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27899452},
      pmc          = {pmc:PMC5247653},
      doi          = {10.1074/jbc.M116.759944},
      url          = {https://pub.dzne.de/record/276852},
}