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High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1
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| Zeitschriftentitel: | Molecular Oncology |
|---|---|
| Personen und Körperschaften: | , , , , , , , , , , |
| In: | Molecular Oncology, 13, 2019, 4, S. 811-828 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Liao, Lili Alicea‐Velázquez, Nilda L. Langbein, Lauren Niu, Xiaohua Cai, Weijia Cho, Eun‐Ah Zhang, Meiling Greer, Celeste B. Yan, Qin Cosgrove, Michael S. Yang, Haifeng Liao, Lili Alicea‐Velázquez, Nilda L. Langbein, Lauren Niu, Xiaohua Cai, Weijia Cho, Eun‐Ah Zhang, Meiling Greer, Celeste B. Yan, Qin Cosgrove, Michael S. Yang, Haifeng |
|---|---|
| author |
Liao, Lili Alicea‐Velázquez, Nilda L. Langbein, Lauren Niu, Xiaohua Cai, Weijia Cho, Eun‐Ah Zhang, Meiling Greer, Celeste B. Yan, Qin Cosgrove, Michael S. Yang, Haifeng |
| spellingShingle |
Liao, Lili Alicea‐Velázquez, Nilda L. Langbein, Lauren Niu, Xiaohua Cai, Weijia Cho, Eun‐Ah Zhang, Meiling Greer, Celeste B. Yan, Qin Cosgrove, Michael S. Yang, Haifeng Molecular Oncology High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 Cancer Research Genetics Molecular Medicine General Medicine Oncology |
| author_sort |
liao, lili |
| spelling |
Liao, Lili Alicea‐Velázquez, Nilda L. Langbein, Lauren Niu, Xiaohua Cai, Weijia Cho, Eun‐Ah Zhang, Meiling Greer, Celeste B. Yan, Qin Cosgrove, Michael S. Yang, Haifeng 1574-7891 1878-0261 Wiley Cancer Research Genetics Molecular Medicine General Medicine Oncology http://dx.doi.org/10.1002/1878-0261.12434 <jats:p>Polybromo‐1 (<jats:styled-content style="fixed-case">PBRM</jats:styled-content>1) is an important tumor suppressor in kidney cancer. It contains six tandem bromodomains (<jats:styled-content style="fixed-case">BD</jats:styled-content>s), which are specialized structures that recognize acetyl‐lysine residues. While <jats:styled-content style="fixed-case">BD</jats:styled-content>2 has been found to bind acetylated histone H3 lysine 14 (H3K14ac), it is not known whether other <jats:styled-content style="fixed-case">BD</jats:styled-content>s collaborate with <jats:styled-content style="fixed-case">BD</jats:styled-content>2 to generate strong binding to H3K14ac, and the importance of H3K14ac recognition for the molecular and tumor suppressor function of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 is also unknown. We discovered that full‐length <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1, but not its individual <jats:styled-content style="fixed-case">BD</jats:styled-content>s, strongly binds H3K14ac. <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 were found to collaborate to facilitate strong binding to H3K14ac. Quantitative measurement of the interactions between purified <jats:styled-content style="fixed-case">BD</jats:styled-content> proteins and H3K14ac or nonacetylated peptides confirmed the tight and specific association of the former. Interestingly, while the structural integrity of <jats:styled-content style="fixed-case">BD</jats:styled-content>4 was found to be required for H3K14ac recognition, the conserved acetyl‐lysine binding site of <jats:styled-content style="fixed-case">BD</jats:styled-content>4 was not. Furthermore, simultaneous point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 prevented recognition of H3K14ac, altered promoter binding and gene expression, and caused <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 to relocalize to the cytoplasm. In contrast, tumor‐derived point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone lowered <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1's affinity to H3K14ac and also disrupted promoter binding and gene expression without altering cellular localization. Finally, overexpression of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 variants containing point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 or <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone failed to suppress tumor growth in a xenograft model. Taken together, our study demonstrates that <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 collaborate to generate high affinity to H3K14ac and tether <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 to chromatin. Mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone weaken these interactions, and this is sufficient to abolish its molecular and tumor suppressor functions.</jats:p> High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of <scp>PBRM</scp>1 Molecular Oncology |
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10.1002/1878-0261.12434 |
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Wiley, 2019 |
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Wiley, 2019 |
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1574-7891 1878-0261 |
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Molecular Oncology |
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| title |
High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| title_unstemmed |
High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| title_full |
High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| title_fullStr |
High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| title_full_unstemmed |
High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| title_short |
High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| title_sort |
high affinity binding of h3k14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of <scp>pbrm</scp>1 |
| topic |
Cancer Research Genetics Molecular Medicine General Medicine Oncology |
| url |
http://dx.doi.org/10.1002/1878-0261.12434 |
| publishDate |
2019 |
| physical |
811-828 |
| description |
<jats:p>Polybromo‐1 (<jats:styled-content style="fixed-case">PBRM</jats:styled-content>1) is an important tumor suppressor in kidney cancer. It contains six tandem bromodomains (<jats:styled-content style="fixed-case">BD</jats:styled-content>s), which are specialized structures that recognize acetyl‐lysine residues. While <jats:styled-content style="fixed-case">BD</jats:styled-content>2 has been found to bind acetylated histone H3 lysine 14 (H3K14ac), it is not known whether other <jats:styled-content style="fixed-case">BD</jats:styled-content>s collaborate with <jats:styled-content style="fixed-case">BD</jats:styled-content>2 to generate strong binding to H3K14ac, and the importance of H3K14ac recognition for the molecular and tumor suppressor function of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 is also unknown. We discovered that full‐length <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1, but not its individual <jats:styled-content style="fixed-case">BD</jats:styled-content>s, strongly binds H3K14ac. <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 were found to collaborate to facilitate strong binding to H3K14ac. Quantitative measurement of the interactions between purified <jats:styled-content style="fixed-case">BD</jats:styled-content> proteins and H3K14ac or nonacetylated peptides confirmed the tight and specific association of the former. Interestingly, while the structural integrity of <jats:styled-content style="fixed-case">BD</jats:styled-content>4 was found to be required for H3K14ac recognition, the conserved acetyl‐lysine binding site of <jats:styled-content style="fixed-case">BD</jats:styled-content>4 was not. Furthermore, simultaneous point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 prevented recognition of H3K14ac, altered promoter binding and gene expression, and caused <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 to relocalize to the cytoplasm. In contrast, tumor‐derived point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone lowered <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1's affinity to H3K14ac and also disrupted promoter binding and gene expression without altering cellular localization. Finally, overexpression of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 variants containing point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 or <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone failed to suppress tumor growth in a xenograft model. Taken together, our study demonstrates that <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 collaborate to generate high affinity to H3K14ac and tether <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 to chromatin. Mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone weaken these interactions, and this is sufficient to abolish its molecular and tumor suppressor functions.</jats:p> |
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| description | <jats:p>Polybromo‐1 (<jats:styled-content style="fixed-case">PBRM</jats:styled-content>1) is an important tumor suppressor in kidney cancer. It contains six tandem bromodomains (<jats:styled-content style="fixed-case">BD</jats:styled-content>s), which are specialized structures that recognize acetyl‐lysine residues. While <jats:styled-content style="fixed-case">BD</jats:styled-content>2 has been found to bind acetylated histone H3 lysine 14 (H3K14ac), it is not known whether other <jats:styled-content style="fixed-case">BD</jats:styled-content>s collaborate with <jats:styled-content style="fixed-case">BD</jats:styled-content>2 to generate strong binding to H3K14ac, and the importance of H3K14ac recognition for the molecular and tumor suppressor function of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 is also unknown. We discovered that full‐length <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1, but not its individual <jats:styled-content style="fixed-case">BD</jats:styled-content>s, strongly binds H3K14ac. <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 were found to collaborate to facilitate strong binding to H3K14ac. Quantitative measurement of the interactions between purified <jats:styled-content style="fixed-case">BD</jats:styled-content> proteins and H3K14ac or nonacetylated peptides confirmed the tight and specific association of the former. Interestingly, while the structural integrity of <jats:styled-content style="fixed-case">BD</jats:styled-content>4 was found to be required for H3K14ac recognition, the conserved acetyl‐lysine binding site of <jats:styled-content style="fixed-case">BD</jats:styled-content>4 was not. Furthermore, simultaneous point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 prevented recognition of H3K14ac, altered promoter binding and gene expression, and caused <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 to relocalize to the cytoplasm. In contrast, tumor‐derived point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone lowered <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1's affinity to H3K14ac and also disrupted promoter binding and gene expression without altering cellular localization. Finally, overexpression of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 variants containing point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 or <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone failed to suppress tumor growth in a xenograft model. Taken together, our study demonstrates that <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 collaborate to generate high affinity to H3K14ac and tether <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 to chromatin. Mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone weaken these interactions, and this is sufficient to abolish its molecular and tumor suppressor functions.</jats:p> |
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| spelling | Liao, Lili Alicea‐Velázquez, Nilda L. Langbein, Lauren Niu, Xiaohua Cai, Weijia Cho, Eun‐Ah Zhang, Meiling Greer, Celeste B. Yan, Qin Cosgrove, Michael S. Yang, Haifeng 1574-7891 1878-0261 Wiley Cancer Research Genetics Molecular Medicine General Medicine Oncology http://dx.doi.org/10.1002/1878-0261.12434 <jats:p>Polybromo‐1 (<jats:styled-content style="fixed-case">PBRM</jats:styled-content>1) is an important tumor suppressor in kidney cancer. It contains six tandem bromodomains (<jats:styled-content style="fixed-case">BD</jats:styled-content>s), which are specialized structures that recognize acetyl‐lysine residues. While <jats:styled-content style="fixed-case">BD</jats:styled-content>2 has been found to bind acetylated histone H3 lysine 14 (H3K14ac), it is not known whether other <jats:styled-content style="fixed-case">BD</jats:styled-content>s collaborate with <jats:styled-content style="fixed-case">BD</jats:styled-content>2 to generate strong binding to H3K14ac, and the importance of H3K14ac recognition for the molecular and tumor suppressor function of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 is also unknown. We discovered that full‐length <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1, but not its individual <jats:styled-content style="fixed-case">BD</jats:styled-content>s, strongly binds H3K14ac. <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 were found to collaborate to facilitate strong binding to H3K14ac. Quantitative measurement of the interactions between purified <jats:styled-content style="fixed-case">BD</jats:styled-content> proteins and H3K14ac or nonacetylated peptides confirmed the tight and specific association of the former. Interestingly, while the structural integrity of <jats:styled-content style="fixed-case">BD</jats:styled-content>4 was found to be required for H3K14ac recognition, the conserved acetyl‐lysine binding site of <jats:styled-content style="fixed-case">BD</jats:styled-content>4 was not. Furthermore, simultaneous point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 prevented recognition of H3K14ac, altered promoter binding and gene expression, and caused <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 to relocalize to the cytoplasm. In contrast, tumor‐derived point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone lowered <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1's affinity to H3K14ac and also disrupted promoter binding and gene expression without altering cellular localization. Finally, overexpression of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 variants containing point mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 or <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone failed to suppress tumor growth in a xenograft model. Taken together, our study demonstrates that <jats:styled-content style="fixed-case">BD</jats:styled-content>s 2, 4, and 5 of <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 collaborate to generate high affinity to H3K14ac and tether <jats:styled-content style="fixed-case">PBRM</jats:styled-content>1 to chromatin. Mutations in <jats:styled-content style="fixed-case">BD</jats:styled-content>2 alone weaken these interactions, and this is sufficient to abolish its molecular and tumor suppressor functions.</jats:p> High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of <scp>PBRM</scp>1 Molecular Oncology |
| spellingShingle | Liao, Lili, Alicea‐Velázquez, Nilda L., Langbein, Lauren, Niu, Xiaohua, Cai, Weijia, Cho, Eun‐Ah, Zhang, Meiling, Greer, Celeste B., Yan, Qin, Cosgrove, Michael S., Yang, Haifeng, Molecular Oncology, High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1, Cancer Research, Genetics, Molecular Medicine, General Medicine, Oncology |
| title | High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| title_full | High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| title_fullStr | High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| title_full_unstemmed | High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| title_short | High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| title_sort | high affinity binding of h3k14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of <scp>pbrm</scp>1 |
| title_unstemmed | High affinity binding of H3K14ac through collaboration of bromodomains 2, 4 and 5 is critical for the molecular and tumor suppressor functions of PBRM1 |
| topic | Cancer Research, Genetics, Molecular Medicine, General Medicine, Oncology |
| url | http://dx.doi.org/10.1002/1878-0261.12434 |