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Molecular and Cellular Biology, July 2000, p. 5276-5284, Vol. 20, No. 14
Department of Developmental
Therapeutics1 and Department of
Genetics,3 Medicine Branch, Division of
Clinical Sciences, National Cancer Institute, Bethesda, Maryland 20889, and Department of Cell Biology, Vanderbilt University School
of Medicine, Nashville, Tennessee 37232-21752
Received 31 January 2000/Returned for modification 15 March
2000/Accepted 12 April 2000
Somatic mutations at Thr-58 of c-Myc have been detected in
Burkitt's lymphoma (BL) tumors and have been shown to affect the transforming potential of the Myc oncoprotein. In addition, the N-terminal domain of c-Myc has been shown to interact with microtubules in vivo, and the binding of c-Myc to
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Copyright © 2000, American Society for Microbiology. All rights reserved.
Disruption of Myc-Tubulin Interaction by Hyperphosphorylation of
c-Myc during Mitosis or by Constitutive Hyperphosphorylation of
Mutant c-Myc in Burkitt's Lymphoma

-tubulin was localized to amino
acids 48 to 135 within the c-Myc protein. We demonstrate that c-Myc
proteins harboring a naturally occurring mutation at Thr-58 from BL
cell lines have increased stability and are constitutively hyperphosphorylated, which disrupts the in vivo
interaction of c-Myc with
-tubulin. In addition, we show that
wild-type c-Myc-
-tubulin interactions are also disrupted during a
transient mitosis-specific hyperphosphorylation of
c-Myc, which resembles the constitutive hyperphosphorylation pattern of Thr-58 in BL cells.
*
Corresponding author. Mailing address: NCI-Navy
Oncology Branch, Bldg. 8, R 5101, Bethesda, MD 20889. Phone: (301)
402-0082. Fax: (301) 480-0977. E-mail:
Kayem{at}exchange.nih.gov.
Present address: Department of Thoracic Surgery, Medical
School, Bialystok, Poland.
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