https://www.cell.com/cell/pdf/0092-8674(87)90585-X.pdf

Expression of a single transfected cDNA converts fibroblasts to myoblasts.

https://www.cell.com/cell/pdf/0092-8674(92)90123-T.pdf

Induction of apoptosis in fibroblasts by c-myc protein

A new DNA binding and dimerization motif in immunoglobulin enhancer binding, daughterless, MyoD, and myc proteins

Molecular themes in oncogenesis

Nucleic acid molecules capable of hybridizing under stringent conditions to the nucleotide sequence residing between positions 1 and 453 of the max cDNAs shown in Figure 2, or to the nucleotide sequence reisiding between positions 148 and 810 of the mad cDNAs shown in Figure 14. The Max polypeptide when associated with the Myc or Mad polypeptide is capable of binding to nucleotide sequences containing CACGTG.

https://science.sciencemag.org/content/sci/251/4998/1211.full.pdf

Max: a helix-loop-helix zipper protein that forms a sequence-specific dna-binding complex with myc and mad

To study the relationship between the primary structure of the c-myc protein and some of its functional properties, we made in-frame insertion and deletion mutants of the normal human c-myc coding domain that was expressed from a retroviral promoter-enhancer. We assessed the effects of these mutations on the ability of c-myc protein to cotransform normal rat embryo cells with a mutant ras gene, induce foci in a Rat-1-derived cell line (Rat-1a), and localize in nuclei. Using the cotransformation assay, we found two regions of the protein (amino acids 105 to 143 and 321 to 439) where integrity was critical: one region (amino acids 1 to 104) that tolerated insertion and small deletion mutations, but not large deletions, and another region (amino acids 144) to 320) that was largely dispensable. Comparison with regions that were important for transformation of Rat-1a cells revealed that some are essential for both activities, but others are important for only one or the other, suggesting that the two assays require different properties of the c-myc protein. Deletion of each of three regions of the c-myc protein (amino acids 106 to 143, 320 to 368, and 370 to 412) resulted in partial cytoplasmic localization, as determined by immunofluorescence or immunoprecipitation following subcellular fractionation. Some abnormally located proteins retained transforming activity; most proteins lacking transforming activity appeared to be normally located.

Definition of regions in human c-myc that are involved in transformation and nuclear localization

https://www.cell.com/cell/pdf/0092-8674(84)90271-X.pdf

Hormonal regulation of the rous sarcoma virus src gene via a heterologous promoter defines a threshold dose for cellular transformation

Weassessed theeffects ofthese mutations ontheability ofc-mycprotein tocotransform normal ratembryo cells withamutant rasgene, induce foci inaRat-l-derived cell line (Rat-la), andlocalize innuclei. Using thecotransformation assay, wefound tworegions oftheprotein (amino acids 105to143and321to439)whereintegrity wascritical: oneregion (amino acids 1to104)that tolerated insertion andsmall deletion mutations, butnotlarge deletions, andanother region (amino acids 144 to320)thatwaslargely dispensable. Comparison withregions thatwereimportant fortransformation of Rat-la cells revealed thatsomeareessential forbothactivities, butothers areimportant foronlyoneorthe other, suggesting that thetwoassays require different properties ofthec-mycprotein. Deletion ofeachofthree regions ofthec-myc protein (amino acids 106to143, 320to368, and370to412)resulted inpartial cytoplasmic localization, asdetermined byimmunofluorescence orimmunoprecipitation

Edward B. Jakobovits

Papers

Definition of regions in human c-myc that are involved in transformation and nuclear localization

Hormonal regulation of the rous sarcoma virus src gene via a heterologous promoter defines a threshold dose for cellular transformation

Definition ofRegions inHumanc-mycThatAreInvolved in Transformation andNuclear Localization