Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity

Yang, Xiuna; Morita, Masahiro; Wang, Hui; Suzuki, Toru; Yang, Wen; Luo, Yunhai; Zhao, Cong; Yu, Yue; Bartlam, Mark; Yamamoto, Tadashi; Rao, Zihe

doi:10.1093/nar/gkn825

Cited by 45 publications

(73 citation statements)

References 58 publications

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“…Recently, several crystal structures of the conserved domains of BTG2 and Tob1 in complex with CNOT7 have been published (Yang et al, 2008;Horiuchi et al, 2009). As expected, these protein structures indicate that the BTG domain structure is highly conserved.…”

Section: The Conserved Btg Domain: Function In the Regulation Of Transupporting

confidence: 60%

“…Interestingly, this model shows that residues of Box A and Box B in the BTG domain are both located in a region contacting the interaction surface with CNOT7 (Horiuchi et al, 2009). Consistent with this notion, amino acid substitutions of residues in both Box A and Box B in these regions of BTG2 and Tob1 interfere with the interaction with CNOT7 (Yang et al, 2008;Horiuchi et al, 2009) (R. Brierley and G.S. Winkler, unpublished observations).…”

Section: The Conserved Btg Domain: Function In the Regulation Of Tranmentioning

confidence: 67%

“…This model would suggest that the BTG domain interacts with the CNOT7 away from the deadenylase active site. However, whereas the interaction with CNOT7 is required for the function of BTG2 and Tob1 in RNA turnover, purified BTG2 can inhibit the deadenylase activity of CNOT7 in vitro (Funakoshi et al, 2007;Mauxion et al, 2008;Yang et al, 2008). By contrast, a purified fragment of Tob1 comprising the BTG domain does not inhibit the deadenylase activity of CNOT7 (Horiuchi et al, 2009 …”

Section: The Conserved Btg Domain: Function In the Regulation Of Tranmentioning

confidence: 99%

“…[Color figure can be viewed in the online issue, which is available at www.interscience.wiley.com.] (Yang et al, 2008). B: Relationship between members of the human BTG/Tob family.…”

Section: Functions Of the Divergent C-terminal Regions Functions Of Tmentioning

confidence: 99%

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The mammalian anti‐proliferative BTG/Tob protein family

Winkler

2009

Journal Cellular Physiology

256

246

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The mammalian BTG/Tob family comprises six proteins (BTG1, BTG2/PC3/Tis21, BTG3/ANA, BTG4/PC3B, Tob1/Tob and Tob2), which regulate cell cycle progression in a variety of cell types. They are characterised by the conserved N-terminal domain spanning 104-106 amino acids. Recent biochemical and structural data indicate that the conserved BTG domain is a protein-protein interaction module, which is capable of binding to DNA-binding transcription factors as well as the paralogues CNOT7 (human Caf1/Caf1a) and CNOT8 (human Pop2/Calif/Caf1b), two deadenylase subunits of the Ccr4-Not complex. Consistent with this finding, several members of the BTG/Tob family are shown to be implicated in transcription in the nucleus and cytoplasmic mRNA deadenylation and turnover. The C-terminal regions are less conserved and appear to mediate protein-protein interactions that are unique to each family member. The human and mouse BTG/Tob proteins will be the focus of this review and structural aspects of BTG/Tob interactions with components of the Ccr4-Not complex, and the role of the BTG/Tob proteins in the regulation of gene expression, tumourigenesis and cancer will be discussed.

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Section: The Conserved Btg Domain: Function In the Regulation Of Transupporting

confidence: 60%

Section: The Conserved Btg Domain: Function In the Regulation Of Tranmentioning

confidence: 67%

Section: The Conserved Btg Domain: Function In the Regulation Of Tranmentioning

confidence: 99%

“…[Color figure can be viewed in the online issue, which is available at www.interscience.wiley.com.] (Yang et al, 2008). B: Relationship between members of the human BTG/Tob family.…”

Section: Functions Of the Divergent C-terminal Regions Functions Of Tmentioning

confidence: 99%

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The mammalian anti‐proliferative BTG/Tob protein family

Winkler

2009

Journal Cellular Physiology

256

246

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“…4A) (Guéhenneux et al, 1997;Yang et al, 2008). Box A, also known as GR (for growth regulatory), is composed of strand β1, the short helix α3, part of the α2 helix and a connecting loop between them.…”

Section: The Tob/btg Antiproliferative Proteinsmentioning

confidence: 99%

The structural basis for deadenylation by the CCR4-NOT complex

Bartlam

Yamamoto

2010

Protein Cell

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The CCR4-NOT complex is a highly conserved, multifunctional machinery controlling mRNA metabolism. Its components have been implicated in several aspects of mRNA and protein expression, including transcription initiation, elongation, mRNA degradation, ubiquitination, and protein modification. In this review, we will focus on the role of the CCR4-NOT complex in mRNA degradation. The complex contains two types of deadenylase enzymes, one belonging to the DEDD-type family and one belonging to the EEP-type family, which shorten the poly(A) tails of mRNA. We will review the present state of structure-function analyses into the CCR4-NOT deadenylases and summarize current understanding of their roles in mRNA degradation. We will also review structural and functional work on the Tob/BTG family of proteins, which are known to interact with the CCR4-NOT complex and which have been reported to suppress deadenylase activity in vitro.

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Structure of the human Ccr4‐Not nuclease module using X‐ray crystallography and electron paramagnetic resonance spectroscopy distance measurements

et al. 2022

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Regulated degradation of mature, cytoplasmic mRNA is a key step in eukaryotic gene regulation. This process is typically initiated by the recruitment of deadenylase enzymes by cis-acting elements in the 3' untranslated region resulting in the shortening and removal of the 3 0 poly(A) tail of the target mRNA. The Ccr4-Not complex, a major eukaryotic deadenylase, contains two exoribonuclease subunits with selectivity toward poly(A): Caf1 and Ccr4. The Caf1 deadenylase subunit binds the MIF4G domain of the large subunit CNOT1 (Not1) that is the scaffold of the complex. The Ccr4 nuclease is connected to the complex via its leucine-rich repeat (LRR) domain, which binds Caf1, whereas the catalytic activity of Ccr4 is provided by its EEP domain. While the relative positions of the MIF4G domain of CNOT1, the Caf1 subunit, and the LRR domain of Ccr4 are clearly defined in current models, the position of the EEP nuclease domain of Ccr4 is ambiguous. Here, we use X-ray crystallography, the AlphaFold resource of predicted protein structures, and pulse electron paramagnetic resonance spectroscopy to determine and validate the position of the EEP nuclease domain of Ccr4 resulting in an improved model of the human Ccr4-Not nuclease module.

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Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity

Cited by 45 publications

References 58 publications

The mammalian anti‐proliferative BTG/Tob protein family

The mammalian anti‐proliferative BTG/Tob protein family

The structural basis for deadenylation by the CCR4-NOT complex

Structure of the human Ccr4‐Not nuclease module using X‐ray crystallography and electron paramagnetic resonance spectroscopy distance measurements

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