1994
DOI: 10.1128/mcb.14.10.6868
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Modulation of erbB kinase activity and oncogenic potential by single point mutations in the glycine loop of the catalytic domain.

Abstract: Avian c-erbB is activated to a leukemia oncogene following truncation of its amino-terminal ligand-binding domain by retroviral insertion. The insertionally activated transcripts encode protein products which have constitutive tyrosine kinase activity and can induce erythroleukemia but not sarcomas. We have previously found that a valine-to-isoleucine point mutation at position 157 (V1571 mutant) within the tyrosine kinase domain of this truncated erbB can dramatically activate the sarcomagenic potential of th… Show more

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Cited by 14 publications
(15 citation statements)
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References 51 publications
(45 reference statements)
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“…Both mutations change a valine to an isoleucine in the highly conserved glycine rich ATPbinding pocket. Detailed studies of the c-erbB mutation, V157I, have been performed (Shu et al, 1990(Shu et al, , 1991(Shu et al, , 1994). These observations demonstrate that there are several conserved codons in the tyrosine kinase domain which, when mutated, lead to uncontrolled cellular proliferation.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…Both mutations change a valine to an isoleucine in the highly conserved glycine rich ATPbinding pocket. Detailed studies of the c-erbB mutation, V157I, have been performed (Shu et al, 1990(Shu et al, , 1991(Shu et al, , 1994). These observations demonstrate that there are several conserved codons in the tyrosine kinase domain which, when mutated, lead to uncontrolled cellular proliferation.…”
Section: Discussionmentioning
confidence: 99%
“…The V1110I mutation was located in the highly conserved, glycinerich, ATP-binding region of the tyrosine kinase domain. Previously, an activating mutation was detected at an homologous codon in the chicken proto-oncogene, c-erbB (V157I) (Figure 1) (Shu et al, 1990(Shu et al, , 1991(Shu et al, , 1994. The amino acid changes, valine?isoleucine, were identical in the MET and cerbB mutations.…”
Section: Novel Mutations In the Met Proto-oncogenementioning
confidence: 99%
“…Transforming assays performed on Tpr-Met and Tpr-Ron kinase-swapped chimeras indicate that the lack of Ron oncogenic potential is intrinsic to its tyrosine kinase domain. The integrity of the glycine loop motif involved in ATP binding is known to be critical for transformation mediated by p60 c-src and ErbB (27,47). For this reason, we tested the affinity of Tpr-Ron and Tpr-Met for ATP binding.…”
Section: Discussionmentioning
confidence: 99%
“…PCR was performed by KOD plus polymerase (Takara) with primers 5Ј-GAATTC ACC -ATGGAGCGGCGCTG-3Ј (forward) and 5Ј-GTCGACGTCCTTGAATCCC TG -AATACT-3Ј (reverse), and cloned in frame into the EcoRI and SalI site of pCMVTag4A (Stratagene) to generate FLAG-tagged WT-EphA1, and also into pEGFP-N3 (Clontech) to generate GFP-tagged EphA1. The kinase dead (KD) form of EphA1, in which valine 638 in the ATP-binding region was changed to arginine (V638R) (Shamah et al, 2001;Shu et al, 1994), was prepared with primers 5Ј-GACACTGTCATAGGAGAAGGAGAGTTTGGGGAACGGTAT-3Ј (forward) and 5Ј-GTCGACGTCCTTGAATCCCTGAATACT-3Ј (reverse). The PCR product was digested with Tth111I and SalI, and replaced by the corresponding sequence of WTEphA1.…”
Section: Plasmid Constructionmentioning
confidence: 99%