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Ksr1  -  kinase suppressor of ras 1

Mus musculus

Synonyms: AW492498, B-KSR1, D11Bhm183e, D11Bhm184e, Kinase suppressor of Ras 1, ...
 
 
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High impact information on Ksr1

  • Moreover, B-KSR1 mutants defective in MEK binding were unable to augment neurite outgrowth [1].
  • Further examination of the MEK-B-KSR1 interaction revealed that all genetically identified loss-of-function mutations in the catalytic domain severely diminished MEK binding [1].
  • Together, these findings demonstrate the functional importance of MEK binding and indicate that B-KSR1 may function to transduce Ras-dependent signals that are required for neuronal differentiation or that are involved in the normal functioning of the mature central nervous system [1].
  • New studies now provide evidence that Ksr is important for signal transmission within the MAP kinase module, where it apparently acts as a location-regulated scaffold connecting MEK to Raf [2].
  • For the Hb-specific T cell 3.L2, substitution reduces the potency of the ligand 1000-fold [3].
 

Biological context of Ksr1

  • To better understand TCR discrimination of multiple ligands, we have analyzed the crystal structures of two Hb peptide/I-E(k) complexes that differ by only a single amino acid substitution at the P6 anchor position within the peptide (E73D) [3].
  • The interspecies conservation of the chromosome segment comprising c and Hb beta thus extends outside the rodent family [4].
  • Genetic linkage between the albino (c) and hemoglobin beta-chain (Hb beta) genes in rabbits was demonstrated by means of segregation data from one full-sib family [4].
 

Associations of Ksr1 with chemical compounds

 

Other interactions of Ksr1

  • Ksr is a kinase with similarities to the three conserved regions of Raf kinases, especially within the kinase domain [6].
 

Analytical, diagnostic and therapeutic context of Ksr1

References

  1. Identification of B-KSR1, a novel brain-specific isoform of KSR1 that functions in neuronal signaling. Müller, J., Cacace, A.M., Lyons, W.E., McGill, C.B., Morrison, D.K. Mol. Cell. Biol. (2000) [Pubmed]
  2. MAP kinase module: the Ksr connection. Roy, F., Therrien, M. Curr. Biol. (2002) [Pubmed]
  3. Structural and functional consequences of altering a peptide MHC anchor residue. Kersh, G.J., Miley, M.J., Nelson, C.A., Grakoui, A., Horvath, S., Donermeyer, D.L., Kappler, J., Allen, P.M., Fremont, D.H. J. Immunol. (2001) [Pubmed]
  4. Linkage of albino and hemoglobin beta-chain loci in the rabbit. Sandberg, K., Andersson, L. J. Hered. (1987) [Pubmed]
  5. 5,6-Dichloro-1-beta-D-ribofuranosylbenzimidazole inhibits transcription of the beta-hemoglobin gene in vivo at initiation. Mukherjee, R., Molloy, G.R. J. Biol. Chem. (1987) [Pubmed]
  6. Murine Ksr interacts with MEK and inhibits Ras-induced transformation. Denouel-Galy, A., Douville, E.M., Warne, P.H., Papin, C., Laugier, D., Calothy, G., Downward, J., Eychène, A. Curr. Biol. (1998) [Pubmed]
 
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