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Structural and compositional diversity in the kainate receptor family.
Selvakumar, Purushotham; Lee, Joon; Khanra, Nandish; He, Changhao; Munguba, Hermany; Kiese, Lisa; Broichhagen, Johannes; Reiner, Andreas; Levitz, Joshua; Meyerson, Joel R.
Afiliación
  • Selvakumar P; Department of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
  • Lee J; Department of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA.
  • Khanra N; Department of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
  • He C; Department of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA.
  • Munguba H; Department of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA.
  • Kiese L; Department of Biology and Biotechnology, Ruhr University Bochum, Bochum, Germany.
  • Broichhagen J; Leibniz-Forschungsinstitut für Molekulare Pharmakologie, 13125 Berlin, Germany.
  • Reiner A; Department of Biology and Biotechnology, Ruhr University Bochum, Bochum, Germany.
  • Levitz J; Department of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA. Electronic address: jtl2003@med.cornell.edu.
  • Meyerson JR; Department of Physiology and Biophysics, Weill Cornell Medical College, New York, NY 10065, USA. Electronic address: jrm2008@med.cornell.edu.
Cell Rep ; 37(4): 109891, 2021 10 26.
Article en En | MEDLINE | ID: mdl-34706237
The kainate receptors (KARs) are members of the ionotropic glutamate receptor family and assemble into tetramers from a pool of five subunit types (GluK1-5). Each subunit confers distinct functional properties to a receptor, but the compositional and stoichiometric diversity of KAR tetramers is not well understood. To address this, we first solve the structure of the GluK1 homomer, which enables a systematic assessment of structural compatibility among KAR subunits. Next, we analyze single-cell RNA sequencing data, which reveal extreme diversity in the combinations of two or more KAR subunits co-expressed within the same cell. We then investigate the composition of individual receptor complexes using single-molecule fluorescence techniques and find that di-heteromers assembled from GluK1, GluK2, or GluK3 can form with all possible stoichiometries, while GluK1/K5, GluK2/K5, and GluK3/K5 can form 3:1 or 2:2 complexes. Finally, using three-color single-molecule imaging, we discover that KARs can form tri- and tetra-heteromers.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores de Ácido Kaínico / Multimerización de Proteína Límite: Humans Idioma: En Revista: Cell Rep Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores de Ácido Kaínico / Multimerización de Proteína Límite: Humans Idioma: En Revista: Cell Rep Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos