The c-Myc Oncoprotein Interacts with Bcr

AbstractBcr is a multifunctional protein that is the fusion partner for Abl (p210 Bcr-Abl) in Philadelphia chromosome positive leukemias. We have identified c-Myc as a binding partner for Bcr in both yeast and mammalian cells. We are also able to observe interactions between natively expressed c-Myc and Bcr in leukemic cell lines. Although Bcr and Max have overlapping binding sites on c-Myc, Bcr cannot interact with Max, or with the c-Myc•Max heterodimer. Bcr expression blocks activation of c-Myc-responsive genes, as well as the transformed phenotype induced by coexpression of c-Myc and H-Ras, and this finding suggests that one function of Bcr is to limit the activity of c-Myc. However, Bcr does not block c-Myc function by preventing its nuclear localization. Interestingly, increased Bcr dosage in COS-7 and K-562 cells correlates with a reduction in c-Myc protein levels, suggesting that Bcr may in fact be limiting c-Myc activity by regulating its stability. These data indicate that Bcr is a novel regulator of c-Myc function whose disrupted expression may contribute to the high level of c-Myc protein that is observed in Bcr-Abl transformed cells

Chapter 14: A Memorable Student and Advice to Students/Professionals

In this chapter, Dr. Arlinghaus reflects on his career at MD Anderson, noting that he is very pleased with the people he has trained.He recalls in particular, Guzi Jamjun [SP?], a graduate student from Saudi Arabia who trained at the Graduate School of Biomedical Science.Dr. Arlinghaus describes how Mr. Jamjun was able to help him in his own thinking about laboratory technique and methods, noting how rare it has been for him to find someone to discuss work deeply.At the end of the chapter, Dr. Arlinghaus gives advice to students and professionals: work hard, be honest, only publish what you believe.He also says that he doesn\u27t know how to instill drive and a sense of mission in people, but notes that if it\u27s a hobby, it\u27s not enough. He advises leaders to attract bright people and to listen to them.https://openworks.mdanderson.org/mchv_interviewchapters/1297/thumbnail.jp

Chapter 09: Fellowships and More Creative Research

In this chapter, Dr. Arlinghaus describes the research he conducted under the mentorship of Dr. Richard Schweet while he was on fellowship at the University of Kentucky College of Medicine, Lexington, Kentucky (1962-1963 and 1964 - 1965).Dr. Arlinghaus describes how he came to work on the mechanisms of peptide bond formation in ribosomes in hemoglobin.He describes the theory of this process at the time that long chains of proteins were assembled.Dr. Arlinghaus\u27s research revealed a different and more complex, two-stop mechanism involving ribosomes, messenger RNA and translocation processes.Dr. Arlinghaus notes that this ribosome mechanism is now in textbooks and, at the time, it won him national recognition.He recalls giving a talk in Atlantic City, noting that he wasn\u27t nervous, but confident because I knew what no one in this room knew and I was going to tell them about it. Dr. Arlinghaus states that he had knowledge and creativity and he reflects on where his abilities and research success came from: keeping up with the latest technique, luck, being simple minded, open minded, and aware that thing might be different than reported in textbooks.https://openworks.mdanderson.org/mchv_interviewchapters/1292/thumbnail.jp