Literature DB >> 7935430

Association of MEK1 with p21ras.GMPPNP is dependent on B-Raf.

S A Moodie1, M J Paris, W Kolch, A Wolfman.   

Abstract

We have previously reported that immobilized p21ras forms a GMPPNP-dependent complex with a MEK activity. Furthermore, the association of the MEK activity was found to be independent of the presence of Raf-1. We have extended those observations to show that MEK1 is the MEK activity previously described to associate with immobilized p21ras.GMPPNP. The association between MEK1 and immobilized p21ras.GMPPNP increased its specific activity towards p42MAPK. We detected the specific association of B-Raf with immobilized p21ras.GMPPNP. In contrast to Raf-1-immunodepleted lysates, preclearance of the cytosolic B-Raf significantly reduced, by 96%, the amount of MEK1 activity associated with immobilized p21ras.GMPPNP. The decrease in MEK1 activity correlated with complete loss in the binding of both B-Raf and MEK1 proteins with immobilized p21ras.GMPPNP. These data suggest that the p21ras.GMPPNP-dependent activation of MEK1 in brain extracts is dependent on the presence of the B-Raf protein kinase.

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Year:  1994        PMID： 7935430      PMCID： PMC359249          DOI： 10.1128/mcb.14.11.7153-7162.1994

Source DB:  PubMed          Journal:  Mol Cell Biol        ISSN： 0270-7306            Impact factor:   4.272


  65 in total

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Journal:  Proc Natl Acad Sci U S A       Date:  1993-06-01       Impact factor: 11.205

5.  Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2.

Authors:  P Chardin; J H Camonis; N W Gale; L van Aelst; J Schlessinger; M H Wigler; D Bar-Sagi
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Journal:  Cell       Date:  1993-05-07       Impact factor: 41.582

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  20 in total

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10.  Interruption of the Ras/MEK/ERK signaling cascade enhances Chk1 inhibitor-induced DNA damage in vitro and in vivo in human multiple myeloma cells.

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