Very-KIND is a novel nervous system specific guanine nucleotide exchange factor for Ras GTPases

Anaid Mees, Rebecca Rock, Francesca D. Ciccarelli, Cornelia B. Leberfinger, Johanna M. Borawski, Peer Bork, Stefan Wiese, Manfred Gessler, Eugen Kerkhoff

Research output: Contribution to journalArticlepeer-review


The kinase non-catalytic c-lobe domain (KIND) evolved from the catalytic protein kinase fold into a potential protein interaction module for signalling proteins. Spir family actin organizers and the non-receptor phosphatase type 13 (PTP type 13) encode a KIND domain in the very N-terminal parts of the proteins. Here we report the characterization and cloning of a third member of the KIND protein family, which we have named very-KIND (VKIND) because of its two KIND domains. Like the other members of the protein family, VKIND has a KIND domain at the N-terminus. A second KIND domain is located in the central part of the protein. The C-terminal half encodes a guanine nucleotide exchange factor motif for Ras-like GTPases (RasGEF) and a RasGEF N-terminal module (RasGEFN). There is only one VKIND gene in the mammalian genomes and up to now we have found the gene only in vertebrates. During mouse embryogenesis the VKIND gene was specifically expressed in the developing nervous system. In adult mice Northern hybridizations revealed high expression only in brain. Low expression could be detected in ovary. In situ hybridizations showed a specific expression of VKIND in neuronal cells of the granular and Purkinje cell layers of the cerebellum.

Original languageEnglish
Pages (from-to)79-85
Number of pages7
JournalGene Expression Patterns
Issue number1
Publication statusPublished - Dec 2005


  • Cerebellum
  • KIND
  • Nervous system
  • Ras
  • RasGEF
  • Signal transduction

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology
  • Cellular and Molecular Neuroscience
  • Developmental Neuroscience


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