Expression of v-src and chicken c-src in rat cells demonstrates qualitative differences between pp60v-src and pp60c-src

Parker, Richard C.; Varmus, Harold; Bishop, J. Michael

doi:10.1016/0092-8674(84)90308-8

Cited by 200 publications

(125 citation statements)

References 22 publications

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“…In parallel with MEK activation by v-src, p42MBPK was rapidly activated within (Iba et al, 1984;Parker et al, 1984;Johnson et al, 1985). CEF that overexpress p60csrc do not show a significant alteration in cell morphology.…”

Section: Introductionmentioning

confidence: 93%

Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-transformed cells: signal transduction/transformation-dependent MBP kinases.

Wang

Erikson

1992

MBoC

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We have used myelin basic protein immobilized in sodium dodecyl sulfate-polyacrylamide gels to identify protein kinases after gel electrophoresis, followed by protein kinase reactions. This technique has permitted us to detect three protein kinases in serum-deprived cells transformed by p60src. On induction of cellular transformation by a temperature-sensitive v-src, a p87 protein kinase is activated within 30 min and remains activated in fully transformed cells. The p63 protein kinase is not fully activated until 24 h but remains activated in transformed cells. The commonly studied p42MBPK is rapidly activated within 30 min, and its kinase activity decreases significantly by 24 h, when the p63 enzyme is fully activated. The p42MBPK, as well as the p63 and p87 enzymes, are stimulated by transforming p60c-src mutants but not normal c-src or nonmyristylated p60c-src. In addition, the kinase activity of p63 enzyme, but not of p42MBPK, can be induced in okadaic acid-treated chicken embryo fibroblasts, indicating that phosphatase 2A and/or phosphatase 1 may be involved in the regulation of its activity. Additional data indicate that either p42MBPK or p63 activity correlates with the stimulation of the protein kinase p90RSK. Thus, there may be two independent pathways leading to the activation of the RSK gene product.

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Section: Introductionmentioning

confidence: 93%

Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-transformed cells: signal transduction/transformation-dependent MBP kinases.

Wang

Erikson

1992

MBoC

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“…Cell lines have been obtained that overexpress the cellular src protein after transfection with plasmids containing the c-src coding sequence (Iba et al, 1984;Parker et al, 1984;Shalloway et al, 1984;Johnson et al, 1985;Warren et al, 1988). Examination of the effects of overexpression of pp60 ~-'~ up to a level comparable to that of pp60 v-s~ in RSVtransformed cells, has permitted the demonstration that qualitative differences between the viral and the cellular src proteins must be responsible for the induction of full cellular transformation and in vivo tumorigenicity.…”

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confidence: 99%

Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells.

David‐Pfeuty

Nouvian-Dooghe

1990

The Journal of Cell Biology

129

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The mouse mAb, mAb 327, that recognizes specifically both pp60v-src and pp60c-src in a wide variety of cells, has been used to determine precisely the various locations of pp60c-src in NIH c-src overexpresser cells, using the technique of immunofluorescence microscopy. In interphase cells, the protein exhibits two main distributions: one that appears uniform and in association with the cell surface and the other that is patchy and juxtanuclear and coincides with the centrosomes. The juxtanuclear aggregation of pp60c-src-containing patches depends on microtubules and does not seem to occur within the Golgi apparatus and the rough ER. At the G2-to-M-phase transition, a drastic change in the localization patterns of pp60c-src takes place. We also report experiments in which the NIH c-src overexpresser cells were exposed to Con A for various times to induce a redistribution of the cell surface Con A receptors. We show that, at each stage of the Con A-mediated endocytotic process, the Con A-receptor complexes redistribute into structures to which pp60c-src appears also to be associated: at first, into patches that form at the cell surface level and then, into a cap that stands at the cell center in a juxtanuclear position and that coincides with the Golgi apparatus. During this capping process, pp60c-src-containing vesicles continue to accumulate in a centriolar spot, as in interphase, Con A-untreated cells, from which Con A is excluded. The significance of the intracellular locations of pp60c-src to the possible functions of the protein is discussed. Also, the distribution patterns of the cellular protein in the NIH c-src overexpresser cells are compared with those of pp60v-src in RSV-transformed cells. The differences observed are discussed in relation with the differences in transforming capacities of the two proteins. Finally, the possible physiological significance of the association between pp60c-src and the structures generated after the binding of Con A to its surface receptors is addressed.

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“…Howcver, the effect of proto-oncogene expression in the "wrong" cell at the "wrong" time is not known. On the other band, it was shown that elevation of pp6oc-src kinase activity alone is not sufficient to mediate neoplastic transformation of cells (Parker et al, 1984;Iba et a/., 1984). Another effect of pp60c-s'c in fish tumors might be a qualitative change of the protein, either due to mutational changes in the primary structure or to new unique amino-terminal tyrosine phosphorylation of the pp6oc-.rrc itself, as was shown in a human neuroblastoma cell line (Bolen et a/.…”

Section: Discussionmentioning

confidence: 98%

Comparative studies on the src proto-oncogene and its gene product pp60c-src in normal and neoplastic tissues of lower vertebrates

Barnekow

Schartl

1987

Comparative Biochemistry and Physiology Part B: Comparative Bio

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Abstract-!. Oncogenes appear to play an important role in the physiology of transformedas weil as of normal cells.2. Tbe src oncogene is by far the most investigated oncogene in birds and mam~als wit~ respect t.o the biochemical characteristics of its tyrosine kinase activity, although the specd1c functton of thts enzymatic activity still remains to be uncovered.3. Systematic sturlies on the src related kinase activity in lower animals are lacking.4. To contribute to a better understanding of the function of the c-src gene, we performed a comparative study on lower chordates.

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Expression of v-src and chicken c-src in rat cells demonstrates qualitative differences between pp60v-src and pp60c-src

Cited by 200 publications

References 22 publications

Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-transformed cells: signal transduction/transformation-dependent MBP kinases.

Activation of protein serine/threonine kinases p42, p63, and p87 in Rous sarcoma virus-transformed cells: signal transduction/transformation-dependent MBP kinases.

Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells.

Comparative studies on the src proto-oncogene and its gene product pp60c-src in normal and neoplastic tissues of lower vertebrates

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