L-myc cooperates with ras to transform primary rat embryo fibroblasts.

Birrer, Michael J.; Segal, Shoshana; DeGreve, J; Kaye, Frederick; Sausville, Edward A.; Minna, John D.

doi:10.1128/mcb.8.6.2668

Cited by 90 publications

(73 citation statements)

References 32 publications

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“…In contrast, L-myc is only 1 ± 10% as e ective (Birrer, 1988). It was originally proposed that this was due to L-myc possessing a weaker TAD than either cmyc or N-myc (Barrett et al, 1992).…”

Section: Erential E Ects Of Myc Proteins On Dna Binding Transcripmentioning

confidence: 98%

MYC oncogenes and human neoplastic disease

1999

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c-myc, N-myc and L-myc are the three members of the myc oncoprotein family whose role in the pathogenesis of many human neoplastic diseases has received wide empirical support. In this review, we ®rst summarize data, derived mainly from non-clinical studies, indicating that these oncoproteins actually serve quite di erent roles in vivo. This concept necessarily lies at the heart of the basis for the observation that the deregulated expression of each MYC gene is reproducibly associated with only certain naturally occurring malignancies in humans and that these genes are not interchangeable with respect to their aberrant functional consequences. We also review evidence implicating each of the above MYC genes in speci®c neoplastic diseases and have attempted to identify unresolved questions which deserve further basic or clinical investigation. We have made every attempt to review those diseases for which signi®cant and con®rmatory evidence, based on studies with primary tumor material, exists to implicate MYC members in their causation and/or progression.

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Section: Erential E Ects Of Myc Proteins On Dna Binding Transcripmentioning

confidence: 98%

MYC oncogenes and human neoplastic disease

1999

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“…22 Furthermore, under certain conditions, L-myc can promote the growth of transformed cells as well as, or better than, c-myc. 17 Together, these observations suggest that, while some functions of myc proteins are overlapping and redundant, others are unique.…”

Section: Introductionmentioning

confidence: 96%

“…14 ± 16 This has suggested that the three myc proteins serve different functions, a notion underscored by the finding that L-myc is only 1 ± 10% as efficient as c-myc or N-myc in transforming primary fibroblasts and that it contains a comparatively weak transactivation domain. 17,18 Other evidence for functional differences among the three myc proteins stems from the different phenotypes of c-myc, Nmyc, and L-myc knockout mice, 16,19,20 the association of each myc gene with a distinctive spectrum of naturally occurring neoplasms, 21 and their differential abilities to alter the sensitivity of cells to chemotherapeutic drugs. 22 In contrast, each myc protein is equally effective at enhancing the apoptotic response of hematopoietic cells to growth factor withdrawal.…”

Section: Introductionmentioning

confidence: 99%

Promotion of growth and apoptosis in c-myc nullizygous fibroblasts by other members of the myc oncoprotein family

et al. 2000

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c-myc nullizygous fibroblasts (KO cells) were used to compare the abilities of c-myc, N-myc and L-myc oncoproteins to accelerate growth, promote apoptosis, revert morphology, and regulate the expression of previously described c-myc target genes. All three myc oncoproteins were expressed following retroviral transduction of KO cells. The proteins all enhanced the growth rate of KO cells and significantly shortened the cell cycle transition time. They also accelerated apoptosis following serum deprivation, reverted the abnormal KO cell morphology, and modulated the expression of previously described c-myc target genes. In most cases, Lmyc was equivalent to c-myc and N-myc in restoring all of the c-myc-dependent activities. These findings contrast with the previously reported weak transforming and transactivating properties of L-myc. Myc oncoproteins may thus impart both highly similar as well as dissimilar signals to the cells in which they are expressed. Cell Death and Differentiation (2000) 7, 697 ± 705.

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“…The c-Myc protein exhibits sequence-speci®c DNA binding when dimerized with its partner Max, and DNA binding is mediated through the basic region, which recognizes the core sequence CACGTG (Berberich et al, 1992;Blackwell et al, 1993;Blackwood and Eisenman, 1991;, but exhibits somewhat higher a nity for the more extended sequence ACCACGTGGT (Berberich et al, 1992;Blackwell et al, 1993;Halazonetis and Kandil, 1991). There are three closely related Myc family proteins (c-Myc, N-Myc and L-Myc), each with documented oncogenic potential (Birrer et al, 1988;Schwab et al, 1985;Yancopoulos et al, 1985) and similar DNA binding properties (Mukherjee et al, 1992). For simplicity, we will use the term Myc to refer to all three proteins, but delineate any distinct activities where they apply.…”

mentioning

confidence: 99%