A Novel Human Gene Closely Related to the
            <i>abl</i>
            Proto-Oncogene

Gd, Kruh; King, C. Richter; Kraus, M H; Popescu, N. C.; Amsbaugh, Suzanne C.; Mcbride, Wesley; Aaronson, S A

doi:10.1126/science.3787260

Cited by 81 publications

(31 citation statements)

References 48 publications

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“…A 90 kDa C-terminal domain includes potential actin-and DNA-binding domains, a nuclear localization signal, and binding sites for the adapter proteins Crk/CRKL, Grb2 and Nck Ren et al, 1994). c-Abl and the Arg kinase (product of the abl related gene) share 90 ± 95% identity in the SH2, SH3 and catalytic domains, whereas their C-terminal parts are much more diverse, with only approximately 30% overall identity (Kruh et al, 1986(Kruh et al, , 1990.…”

Section: Introductionmentioning

confidence: 99%

The leukaemic oncoproteins Bcr-Abl and Tel-Abl (ETV6/Abl) have altered substrate preferences and activate similar intracellular signalling pathways

Voß¹,

Posern²,

Hannemann

et al. 2000

Oncogene

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Inappropriate activation of Abl family kinases plays a crucial role in di erent human leukaemias. In addition to the well known oncoproteins p190Bcr-Abl and p210Bcr-Abl, Tel-Abl, a novel fusion protein resulting from a di erent chromosomal translocation, has recently been described. In this study, the kinase speci®cities of the Bcr-Abl and Tel-Abl proteins were compared to the physiological Abl family kinases c-Abl and Arg (abl related gene). Using short peptides which correspond to the target epitopes in known substrate proteins of Abl family kinases, we found a higher catalytic promiscuity of Bcr-Abl and Tel-Abl. Similar to Bcr-Abl, Tel-Abl was found in complexes with the adapter protein CRKL. In addition, c-Crk II and CRKL are tyrosine phosphorylated and complexed with numerous other tyrosine phosphorylated proteins in Tel-Abl expressing Ba/F3 cells. GTPase analysis with a Ras´GTP-speci®c precipitation assay showed constitutive elevation of GTPloaded Ras in cells expressing the leukaemic Abl proteins. The mitogenic MAPK/Erk kinases as well as Akt/PKB, a kinase implicated to negatively regulate apoptosis, were also constitutively activated by both BcrAbl and Tel-Abl. The results indicate that the leukaemic Abl-fusion proteins have catalytic speci®cities di erent from the normal kinases c-Abl and Arg and that Tel-Abl is capable to activate at least some pathways which are also upregulated by Bcr-Abl.

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Section: Introductionmentioning

confidence: 99%

The leukaemic oncoproteins Bcr-Abl and Tel-Abl (ETV6/Abl) have altered substrate preferences and activate similar intracellular signalling pathways

Voß¹,

Posern²,

Hannemann

et al. 2000

Oncogene

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“…The N-terminal regions of c-Abl and Arg share ϳ90% identity and, as found in members of the Src family, contain tandem SH3, 1 SH2, and tyrosine kinase domains (1,2). Recent studies have shown that the cytoplasmic forms of c-Abl and Arg are activated in the cellular response to oxidative stress (3)(4)(5).…”

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confidence: 99%

Glutathione Peroxidase 1 Is Regulated by the c-Abl and Arg Tyrosine Kinases

Cao

Leng

Huang³

et al. 2003

Journal of Biological Chemistry

114

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The c-Abl and Arg tyrosine kinases are activated in the cellular response to oxidative stress. The present studies demonstrate that c-Abl and Arg associate with glutathione peroxidase 1 (GPx1) and that this interaction is regulated by intracellular oxidant levels. The c-Abl and Arg SH3 domains bind directly to a prolinerich site in GPx1 at amino acids 132-145. GPx1 also functions as a substrate for c-Abl-and Arg-mediated phosphorylation on Tyr-96. The results further show that c-Abl and Arg stimulate GPx activity and that these kinases contribute to GPx-mediated protection of cells against oxidative stress. Our findings provide the first evidence that GPx1 is regulated by a signaling pathway that is activated in the oxidative stress response.

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“…The mammalian c-Abl and Arg nonreceptor tyrosine kinases are expressed widely in adult tissues (1)(2)(3). The N-terminal regions of c-Abl and Arg share ϳ90% identity and, as found in members of the Src family, contain tandem Src homology 3 (SH3), 1 SH2, and tyrosine kinase (SH1) domains.…”

mentioning

confidence: 99%