Interaction of MYC with host cell factor-1 is mediated by the evolutionarily conserved Myc box IV motif

The MYC family of oncogenes encodes a set of three related transcription factors that are overexpressed in many human tumors and contribute to the cancer-related deaths of more than 70,000 Americans every year. MYC proteins drive tumorigenesis by interacting with co-factors that enable them to regul...

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Veröffentlicht in:Oncogene 2016-07, Vol.35 (27), p.3613-3618
Hauptverfasser: Thomas, L R, Foshage, A M, Weissmiller, A M, Popay, T M, Grieb, B C, Qualls, S J, Ng, V, Carboneau, B, Lorey, S, Eischen, C M, Tansey, W P
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container_end_page 3618
container_issue 27
container_start_page 3613
container_title Oncogene
container_volume 35
creator Thomas, L R
Foshage, A M
Weissmiller, A M
Popay, T M
Grieb, B C
Qualls, S J
Ng, V
Carboneau, B
Lorey, S
Eischen, C M
Tansey, W P
description The MYC family of oncogenes encodes a set of three related transcription factors that are overexpressed in many human tumors and contribute to the cancer-related deaths of more than 70,000 Americans every year. MYC proteins drive tumorigenesis by interacting with co-factors that enable them to regulate the expression of thousands of genes linked to cell growth, proliferation, metabolism and genome stability. One effective way to identify critical co-factors required for MYC function has been to focus on sequence motifs within MYC that are conserved throughout evolution, on the assumption that their conservation is driven by protein–protein interactions that are vital for MYC activity. In addition to their DNA-binding domains, MYC proteins carry five regions of high sequence conservation known as Myc boxes (Mb). To date, four of the Mb motifs (MbI, MbII, MbIIIa and MbIIIb) have had a molecular function assigned to them, but the precise role of the remaining Mb, MbIV, and the reason for its preservation in vertebrate Myc proteins, is unknown. Here, we show that MbIV is required for the association of MYC with the abundant transcriptional coregulator host cell factor-1 (HCF-1). We show that the invariant core of MbIV resembles the tetrapeptide HCF-binding motif (HBM) found in many HCF-interaction partners, and demonstrate that MYC interacts with HCF-1 in a manner indistinguishable from the prototypical HBM-containing protein VP16. Finally, we show that rationalized point mutations in MYC that disrupt interaction with HCF-1 attenuate the ability of MYC to drive tumorigenesis in mice. Together, these data expose a molecular function for MbIV and indicate that HCF-1 is an important co-factor for MYC.
doi_str_mv 10.1038/onc.2015.416
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We show that the invariant core of MbIV resembles the tetrapeptide HCF-binding motif (HBM) found in many HCF-interaction partners, and demonstrate that MYC interacts with HCF-1 in a manner indistinguishable from the prototypical HBM-containing protein VP16. Finally, we show that rationalized point mutations in MYC that disrupt interaction with HCF-1 attenuate the ability of MYC to drive tumorigenesis in mice. 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MYC proteins drive tumorigenesis by interacting with co-factors that enable them to regulate the expression of thousands of genes linked to cell growth, proliferation, metabolism and genome stability. One effective way to identify critical co-factors required for MYC function has been to focus on sequence motifs within MYC that are conserved throughout evolution, on the assumption that their conservation is driven by protein–protein interactions that are vital for MYC activity. In addition to their DNA-binding domains, MYC proteins carry five regions of high sequence conservation known as Myc boxes (Mb). To date, four of the Mb motifs (MbI, MbII, MbIIIa and MbIIIb) have had a molecular function assigned to them, but the precise role of the remaining Mb, MbIV, and the reason for its preservation in vertebrate Myc proteins, is unknown. Here, we show that MbIV is required for the association of MYC with the abundant transcriptional coregulator host cell factor-1 (HCF-1). We show that the invariant core of MbIV resembles the tetrapeptide HCF-binding motif (HBM) found in many HCF-interaction partners, and demonstrate that MYC interacts with HCF-1 in a manner indistinguishable from the prototypical HBM-containing protein VP16. Finally, we show that rationalized point mutations in MYC that disrupt interaction with HCF-1 attenuate the ability of MYC to drive tumorigenesis in mice. 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13/106
631/45
631/67/395
64/60
82
82/58
Amino Acid Motifs - genetics
Amino Acid Sequence
Animals
Apoptosis
Binding sites
Binding Sites - genetics
Cell Biology
Cell growth
Cell Transformation, Neoplastic - genetics
Conserved sequence
Conserved Sequence - genetics
Evolution, Molecular
Gene expression
Genomes
HEK293 Cells
Host Cell Factor C1 - genetics
Host Cell Factor C1 - metabolism
Human Genetics
Humans
Immunoprecipitation
Internal Medicine
Medicine
Medicine & Public Health
Mice
Mutation
Myc protein
NIH 3T3 Cells
Nucleotide sequence
Oncology
Protein Binding
Protein interaction
Proteins
Proto-Oncogene Proteins c-myc - genetics
Proto-Oncogene Proteins c-myc - metabolism
Sequence Homology, Amino Acid
short-communication
Transcription factors
Tumorigenesis
Tumors
VP16 protein
title Interaction of MYC with host cell factor-1 is mediated by the evolutionarily conserved Myc box IV motif
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