Disruption of Myc-tubulin interaction by hyperphosphorylation of c-Myc during mitosis or by constitutive hyperphosphorylation of mutant c-Myc in Burkitt's lymphoma.

Niklinski J, Claassen G, Meyers C, Gregory MA, Allegra CJ, Kaye FJ, Hann SR, Zajac-Kaye M
Mol Cell Biol. 2000 20 (14): 5276-84

PMID: 10866684 · PMCID: PMC85977 · DOI:10.1128/mcb.20.14.5276-5284.2000

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 alpha-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 alpha-tubulin. In addition, we show that wild-type c-Myc-alpha-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.

MeSH Terms (13)

Amino Acid Substitution Burkitt Lymphoma Cell Line Gene Expression Regulation, Neoplastic Humans Microtubules Mitosis Mutation Peptide Mapping Phosphoproteins Phosphorylation Proto-Oncogene Proteins c-myc Tubulin

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