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      RasGEF1A and RasGEF1B are guanine nucleotide exchange factors that discriminate between Rap GTP-binding proteins and mediate Rap2-specific nucleotide exchange

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      Author
      Yaman, E.
      Gasper, R.
      Koerner, C.
      Wittinghofer, A.
      Tazebay, U. H.
      Date
      2009
      Source Title
      FEBS Journal
      Print ISSN
      1742-464X
      Publisher
      Wiley-Blackwell Publishing Ltd.
      Volume
      276
      Issue
      16
      Pages
      4607 - 4616
      Language
      English
      Type
      Article
      Item Usage Stats
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      212
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      Abstract
      The highly conserved RasGEF1 family of proteins contain a C-terminal CDC25-Ras exchange motif domain and an N-terminal RasGEF-N domain, and are of unknown function and specificity. Using purified RasGEF1A and RasGEF1B proteins, as well as Ras family proteins, we established that RasGEF1A and RasGEF1B function as very specific exchange factors for Rap2, a member of the Rap subfamily of Ras-like G-proteins. They do not act on Rap1 or other members of the Ras subfamily. Although Rap2 was implicated in the regulation of cell adhesion, the establishment of cell morphology, and the modulation of synapses in neurons, no specific guanine nucleotide exchange factor for Rap2 was previously identified. Using reciprocal site-directed mutagenesis, we analyzed residues that allow RasGEF1 proteins to discriminate between Rap1 and Rap2, and we were able to identify Phe39 in the switch I region of Rap2 as a specificity residue. Mutation of the corresponding Ser39 in Rap1 changed the specificity and allowed the nucleotide exchange of Rap1(S39F) to be stimulated by RasGEF1B. © 2009 FEBS.
      Keywords
      G-proteins
      Guanine nucleotide exchange
      Rap2
      Ras family
      RasGEF1
      Guanine nucleotide exchange factor
      Permalink
      http://hdl.handle.net/11693/22668
      Published Version (Please cite this version)
      http://dx.doi.org/10.1111/j.1742-4658.2009.07166.x
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