MM-1, a Novel c-Myc-associating Protein That Represses Transcriptional Activity of c-Myc

Mori, Keisuke; Maeda, Yuichi; Kitaura, Hirotake; Taira, Takahiro; Iguchi‐Ariga, Sanae M.M.; Ariga, Hiroyoshi

doi:10.1074/jbc.273.45.29794

Cited by 105 publications

(131 citation statements)

References 27 publications

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“…Thus, eukaryotic PFD may recognize a broader range of substrates than is currently known (12). Evidence for this notion stems from the finding of additional putative substrates of the eukaryotic chaperone, including the tumor suppressor protein VHL (25), the DNA mismatch repair protein MutH4 (26), and the c-Myc transcription factor (27).…”

Section: Resultsmentioning

confidence: 99%

Molecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin

Lundin

Stirling

Gόmez-Reino

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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Prefoldin (PFD) is a jellyfish-shaped molecular chaperone that has been proposed to play a general role in de novo protein folding in archaea and is known to assist the biogenesis of actins, tubulins, and potentially other proteins in eukaryotes. Using point mutants, chimeras, and intradomain swap variants, we show that the six coiledcoil tentacles of archaeal PFD act in concert to bind and stabilize nonnative proteins near the opening of the cavity they form. Importantly, the interaction between chaperone and substrate depends on the mostly buried interhelical hydrophobic residues of the coiled coils. We also show by electron microscopy that the tentacles can undergo an en bloc movement to accommodate an unfolded substrate. Our data reveal how archael PFD uses its unique architecture and intrinsic coiled-coil properties to interact with nonnative polypeptides.C oiled coils consist of two or more parallel or antiparallel amphipathic ␣-helices that twist around one another to form supercoils (1). The primary sequences of the helices display a heptad repeat (abcdefg), where apolar residues are found preferentially in the first (a) and fourth (d) positions. Although the knobs-into-holes packing of the hydrophobic residues is the predominant stabilizing force for a coiled coil, inter-and intrahelical ionic interactions can act to further stabilize or destabilize its supersecondary structure (1). Coiled coils are found in several molecular chaperones, a diverse family of proteins whose collective cellular role is to ensure the quality control (e.g., folding, assembly, and transport) of nonnative proteins (2, 3). Archaeal prefoldin (PFD) is a chaperone that contains six canonical antiparallel coiled coils whose N-and C-terminal helices project outward from a double ␤-barrel oligomerization domain; the overall shape of the hexameric protein complex, assembled from two PFD␣ and four PFD␤ subunits (␣ 2 ␤ 4 ), resembles a jellyfish with six tentacles (4). In solution, its tentacles are likely to be fully solvated and independently mobile (4). A lower-resolution electron microscope image of recombinant human PFD, which consists of six different proteins (two ␣ class and four ␤ class subunits), reveals that it possesses the same overall structure (5).Like other chaperones, archaeal PFD can selectively interact with and stabilize nonnative (unfolded) polypeptides that expose hydrophobic surfaces in vitro, helping to prevent their aggregation (4, 6, 7). Preliminary studies have shown that deletion of the distal coiled-coil regions in either the ␣ or ␤ subunit abrogates chaperone activity in vitro, implying that PFD grasps its substrates in a multivalent manner (4). Similarly, the eukaryotic PFD-actin complex recently visualized by EM shows that nonnative actin, one of its substrates, makes multiple contacts with the distal regions of the tentacles (5).In the crowded cellular environment, eukaryotic PFD is likely to transiently stabilize ribosome-bound nascent polypeptides (8) before shuttling them to a chaperonin (an ATP-depe...

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Section: Resultsmentioning

confidence: 99%

Molecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin

Lundin

Stirling

Gόmez-Reino

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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“…Other combinations of c-Myc heterodimers have been described that recruit remodeling enzymes, such as HDACs, and exert a repressing effect. Such is the case of MM-1, a novel c-Myc-binding protein that interferes with the E boxdependent transcription activity of c-Myc (Mori et al, 1998). In HeLa cells, c-Myc repression is controlled by a complex containing c-Myc, MM-1, the corepressors mSin3 and TIF1␤, and HDAC1 (Satou et al, 2001).…”

Section: Discussionmentioning

confidence: 99%

Cyclin D1 Is Transcriptionally Down-Regulated by ZO-2 via an E Box and the Transcription Factor c-Myc

Huerta¹,

Muñoz²,

Tapia

et al. 2007

MBoC

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Recent reports have indicated the participation of tight junction (TJ) proteins in the regulation of gene expression and cell proliferation. Here, we have studied the role of zona occludens (ZO)-2, a TJ peripheral protein, in the regulation of cyclin D1 transcription. We found that ZO-2 down-regulates cyclin D1 transcription in a dose-dependent manner. To understand how ZO-2 represses cyclin D1 promoter activity, we used deletion analyses and found that ZO-2 negatively regulates cyclin D1 transcription via an E box and that it diminishes cell proliferation. Because ZO-2 does not associate directly with DNA, electrophoretic mobility shift assay and chromatin immunoprecipitation (ChIP) assay were used to identify the transcription factors mediating the ZO-2-repressive effect. c-Myc was found to bind the E box present in the cyclin D1 promoter, and the overexpression of c-Myc augmented the inhibition generated by ZO-2 transfection. The presence of ZO-2 and c-Myc in the same complex was further demonstrated by immunoprecipitation. ChIP and reporter gene assays using histone deacetylases (HDACs) inhibitors demonstrated that HDACs are necessary for ZO-2 repression and that HDAC1 is recruited to the E box. We conclude that ZO-2 down-regulates cyclin D1 transcription by interacting with the c-Myc/E box element and by recruiting HDAC1.

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“…Two days after transfection, whole cell extracts were prepared by addition of the Triton X-100-containing solution from a Pica gene kit (Wako Pure Chemicals Co. Ltd, Kyoto) to the cells. About one-®fth of the volume of the extract was used for the bgalactosidase assay to normalize the transfection ef®ciency, as described previously (Mori et al 1998;Taira et al 1998) and the luciferase activity due to the reporter plasmid was determined using the Pica gene kit and a luminometer, Luminocounter ATP300 (Advantec Toyo Co. Ltd, Tokyo). The same experiments were repeated ®ve to 10 times.…”

Section: Luciferase Assaymentioning

confidence: 99%

“…Complex formation with various proteins may realize versatile functions of c-Myc, and indeed several proteins have been identi®ed as associating with c-Myc. Max (Blackwood & Eisenman 1991;Blackwood et al 1992), Nmi (Bao & Zervos 1996), YY1 (Shrivastava et al 1993) AP2 (Gaubatz et al 1995), SNF5 (Cheng et al 1999) and CBF/NF-Y (Taira et al 1999) bind to the C-terminal region of c-Myc, while p107 (Beijersbergen et al 1994;Gu et al 1994;Hoang et al 1995), Bin1 (Sakamuro et al 1996), TBP (Hateboer et al 1993;Maheswaran et al 1994), a-tubulin (Alexandrova et al 1995), TRRAP (McMahon et al 1998), Pam (Guo et al 1998), AMY-1 ) and MM-1 (Mori et al 1998) bind to the N-terminal region. Max stimulates the activities of c-Myc in transcription and transformation by heterodimer formation via a leucine zipper (Blackwood & Eisenman 1991;Blackwood et al 1992).…”

Section: Introductionmentioning

confidence: 99%

MSSP promotes ras/myc cooperative cell transforming activity by binding to c‐Myc

Niki¹,

Izumi²,

Saëgusa³

et al. 2000

Genes to Cells

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Background: MSSPs, myc single strand binding proteins, were originally identi®ed as proteins recognizing a putative replication origin/transcriptional enhancer in the human c-Myc gene. The cDNAs encoding four of the family proteins, MSSP-1, MSSP-2, Scr2 and Scr3, were cloned. These proteins carry two copies of the putative RNA binding domains, RNP-A and RNP-B, and have been suggested to participate in DNA replication and cell cycle progression from the G 1 to the S phase.

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MM-1, a Novel c-Myc-associating Protein That Represses Transcriptional Activity of c-Myc

Cited by 105 publications

References 27 publications

Molecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin

Molecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin

Cyclin D1 Is Transcriptionally Down-Regulated by ZO-2 via an E Box and the Transcription Factor c-Myc

MSSP promotes ras/myc cooperative cell transforming activity by binding to c‐Myc

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