Regulating NKX3.1 stability and function: Post-translational modifications and structural determinants
BACKGROUND The androgen‐regulated homeodomain transcription factor NKX3.1 plays roles in early prostate development and functions as a prostate‐specific tumor suppressor. Decreased expression of NKX3.1 protein is common in primary prostate cancer. Discordance between NKX3.1 mRNA and protein levels d...
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| Veröffentlicht in: | The Prostate 2016-05, Vol.76 (6), p.523-533 |
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| container_title | The Prostate |
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| creator | Padmanabhan, Achuth Rao, Varsha De Marzo, Angelo M. Bieberich, Charles J. |
| description | BACKGROUND
The androgen‐regulated homeodomain transcription factor NKX3.1 plays roles in early prostate development and functions as a prostate‐specific tumor suppressor. Decreased expression of NKX3.1 protein is common in primary prostate cancer. Discordance between NKX3.1 mRNA and protein levels during prostate carcinogenesis suggested a key role for post‐transcriptional modifications in regulating NKX3.1 protein levels in prostate epithelial cells. Subsequent studies revealed NKX3.1 to be modified post‐translationally at multiple sites.
METHODS
We reviewed published literature to identify and summarize post‐translational modifications and structural elements critical in regulating NKX3.1 stability and levels in prostate epithelial cells.
RESULTS
NKX3.1 is modified post‐translationally at multiple sites by different protein kinases. These modifications together with several structural determinants were identified to play an important role in NKX3.1 stability and biology.
CONCLUSIONS
In this review, we provide a comprehensive overview of the known post‐translational modifications and structural features that impact NKX3.1. Defining factors that regulate NKX3.1 in prostate epithelial cells will extend our understanding of molecular changes that may contribute to prostate cancer initiation and progression. Prostate 76:523–533, 2016. © 2016 Wiley Periodicals, Inc. |
| doi_str_mv | 10.1002/pros.23144 |
| format | Article |
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The androgen‐regulated homeodomain transcription factor NKX3.1 plays roles in early prostate development and functions as a prostate‐specific tumor suppressor. Decreased expression of NKX3.1 protein is common in primary prostate cancer. Discordance between NKX3.1 mRNA and protein levels during prostate carcinogenesis suggested a key role for post‐transcriptional modifications in regulating NKX3.1 protein levels in prostate epithelial cells. Subsequent studies revealed NKX3.1 to be modified post‐translationally at multiple sites.
METHODS
We reviewed published literature to identify and summarize post‐translational modifications and structural elements critical in regulating NKX3.1 stability and levels in prostate epithelial cells.
RESULTS
NKX3.1 is modified post‐translationally at multiple sites by different protein kinases. These modifications together with several structural determinants were identified to play an important role in NKX3.1 stability and biology.
CONCLUSIONS
In this review, we provide a comprehensive overview of the known post‐translational modifications and structural features that impact NKX3.1. Defining factors that regulate NKX3.1 in prostate epithelial cells will extend our understanding of molecular changes that may contribute to prostate cancer initiation and progression. Prostate 76:523–533, 2016. © 2016 Wiley Periodicals, Inc.</description><identifier>ISSN: 0270-4137</identifier><identifier>EISSN: 1097-0045</identifier><identifier>DOI: 10.1002/pros.23144</identifier><identifier>PMID: 26841725</identifier><identifier>CODEN: PRSTDS</identifier><language>eng</language><publisher>United States: Blackwell Publishing Ltd</publisher><subject>DNA damage and inflammation ; Genes, Tumor Suppressor - physiology ; Homeodomain Proteins - metabolism ; Humans ; Male ; Phosphorylation ; phosphorylation and ubiquitination of NKX3.1 ; prostate cancer ; Prostatic Neoplasms - metabolism ; Prostatic Neoplasms - pathology ; Protein Processing, Post-Translational - physiology ; Protein Stability ; protein turnover and stability ; Transcription Factors - metabolism ; tumor suppressor ; Ubiquitination</subject><ispartof>The Prostate, 2016-05, Vol.76 (6), p.523-533</ispartof><rights>2016 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4304-a880a8ae83084c137171581909d262daa08e3dd745ec313c5ea081a125df46683</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fpros.23144$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fpros.23144$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26841725$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Padmanabhan, Achuth</creatorcontrib><creatorcontrib>Rao, Varsha</creatorcontrib><creatorcontrib>De Marzo, Angelo M.</creatorcontrib><creatorcontrib>Bieberich, Charles J.</creatorcontrib><title>Regulating NKX3.1 stability and function: Post-translational modifications and structural determinants</title><title>The Prostate</title><addtitle>Prostate</addtitle><description>BACKGROUND
The androgen‐regulated homeodomain transcription factor NKX3.1 plays roles in early prostate development and functions as a prostate‐specific tumor suppressor. Decreased expression of NKX3.1 protein is common in primary prostate cancer. Discordance between NKX3.1 mRNA and protein levels during prostate carcinogenesis suggested a key role for post‐transcriptional modifications in regulating NKX3.1 protein levels in prostate epithelial cells. Subsequent studies revealed NKX3.1 to be modified post‐translationally at multiple sites.
METHODS
We reviewed published literature to identify and summarize post‐translational modifications and structural elements critical in regulating NKX3.1 stability and levels in prostate epithelial cells.
RESULTS
NKX3.1 is modified post‐translationally at multiple sites by different protein kinases. These modifications together with several structural determinants were identified to play an important role in NKX3.1 stability and biology.
CONCLUSIONS
In this review, we provide a comprehensive overview of the known post‐translational modifications and structural features that impact NKX3.1. Defining factors that regulate NKX3.1 in prostate epithelial cells will extend our understanding of molecular changes that may contribute to prostate cancer initiation and progression. Prostate 76:523–533, 2016. © 2016 Wiley Periodicals, Inc.</description><subject>DNA damage and inflammation</subject><subject>Genes, Tumor Suppressor - physiology</subject><subject>Homeodomain Proteins - metabolism</subject><subject>Humans</subject><subject>Male</subject><subject>Phosphorylation</subject><subject>phosphorylation and ubiquitination of NKX3.1</subject><subject>prostate cancer</subject><subject>Prostatic Neoplasms - metabolism</subject><subject>Prostatic Neoplasms - pathology</subject><subject>Protein Processing, Post-Translational - physiology</subject><subject>Protein Stability</subject><subject>protein turnover and stability</subject><subject>Transcription Factors - metabolism</subject><subject>tumor suppressor</subject><subject>Ubiquitination</subject><issn>0270-4137</issn><issn>1097-0045</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1PAyEQhonRaP24-APMJp63zgC7UG_G72iqqRq9EVxYg253K7DR_ntpq56AmeedDA8h-whDBKBHM9-FIWXI-RoZIIxEDsCLdTIAKiDnyMQW2Q7hHSDhQDfJFi0lR0GLAakn9q1vdHTtWza-eWFDzELUr65xcZ7p1mR131bRde1xdt-FmEev27Dgu1Y32bQzrnbV8hmWeIi-r2LvU9PYaP3UtbqNYZds1LoJdu_33CFPF-ePp1f57d3l9enJbV5xBjzXUoKW2koGkldpcRRYSBzByNCSGq1BWmaM4IWtGLKqsKmCGmlhal6Wku2Qw9Xc5OSztyGq9673adWgUKQP40jQMlEHv1T_OrVGzbybaj9Xf1oSgCvgyzV2_t9HUAvhaiFcLYWr-8ndw_KWMvkq40K03_8Z7T9UKZgo1PP4UpVnk4czyseqYD_NYYJe</recordid><startdate>20160501</startdate><enddate>20160501</enddate><creator>Padmanabhan, Achuth</creator><creator>Rao, Varsha</creator><creator>De Marzo, Angelo M.</creator><creator>Bieberich, Charles J.</creator><general>Blackwell Publishing Ltd</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7T5</scope><scope>7TO</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20160501</creationdate><title>Regulating NKX3.1 stability and function: Post-translational modifications and structural determinants</title><author>Padmanabhan, Achuth ; Rao, Varsha ; De Marzo, Angelo M. ; Bieberich, Charles J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4304-a880a8ae83084c137171581909d262daa08e3dd745ec313c5ea081a125df46683</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>DNA damage and inflammation</topic><topic>Genes, Tumor Suppressor - physiology</topic><topic>Homeodomain Proteins - metabolism</topic><topic>Humans</topic><topic>Male</topic><topic>Phosphorylation</topic><topic>phosphorylation and ubiquitination of NKX3.1</topic><topic>prostate cancer</topic><topic>Prostatic Neoplasms - metabolism</topic><topic>Prostatic Neoplasms - pathology</topic><topic>Protein Processing, Post-Translational - physiology</topic><topic>Protein Stability</topic><topic>protein turnover and stability</topic><topic>Transcription Factors - metabolism</topic><topic>tumor suppressor</topic><topic>Ubiquitination</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Padmanabhan, Achuth</creatorcontrib><creatorcontrib>Rao, Varsha</creatorcontrib><creatorcontrib>De Marzo, Angelo M.</creatorcontrib><creatorcontrib>Bieberich, Charles J.</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Immunology Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Prostate</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Padmanabhan, Achuth</au><au>Rao, Varsha</au><au>De Marzo, Angelo M.</au><au>Bieberich, Charles J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Regulating NKX3.1 stability and function: Post-translational modifications and structural determinants</atitle><jtitle>The Prostate</jtitle><addtitle>Prostate</addtitle><date>2016-05-01</date><risdate>2016</risdate><volume>76</volume><issue>6</issue><spage>523</spage><epage>533</epage><pages>523-533</pages><issn>0270-4137</issn><eissn>1097-0045</eissn><coden>PRSTDS</coden><abstract>BACKGROUND
The androgen‐regulated homeodomain transcription factor NKX3.1 plays roles in early prostate development and functions as a prostate‐specific tumor suppressor. Decreased expression of NKX3.1 protein is common in primary prostate cancer. Discordance between NKX3.1 mRNA and protein levels during prostate carcinogenesis suggested a key role for post‐transcriptional modifications in regulating NKX3.1 protein levels in prostate epithelial cells. Subsequent studies revealed NKX3.1 to be modified post‐translationally at multiple sites.
METHODS
We reviewed published literature to identify and summarize post‐translational modifications and structural elements critical in regulating NKX3.1 stability and levels in prostate epithelial cells.
RESULTS
NKX3.1 is modified post‐translationally at multiple sites by different protein kinases. These modifications together with several structural determinants were identified to play an important role in NKX3.1 stability and biology.
CONCLUSIONS
In this review, we provide a comprehensive overview of the known post‐translational modifications and structural features that impact NKX3.1. Defining factors that regulate NKX3.1 in prostate epithelial cells will extend our understanding of molecular changes that may contribute to prostate cancer initiation and progression. Prostate 76:523–533, 2016. © 2016 Wiley Periodicals, Inc.</abstract><cop>United States</cop><pub>Blackwell Publishing Ltd</pub><pmid>26841725</pmid><doi>10.1002/pros.23144</doi><tpages>11</tpages></addata></record> |
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| source | MEDLINE; Access via Wiley Online Library |
| subjects | DNA damage and inflammation Genes, Tumor Suppressor - physiology Homeodomain Proteins - metabolism Humans Male Phosphorylation phosphorylation and ubiquitination of NKX3.1 prostate cancer Prostatic Neoplasms - metabolism Prostatic Neoplasms - pathology Protein Processing, Post-Translational - physiology Protein Stability protein turnover and stability Transcription Factors - metabolism tumor suppressor Ubiquitination |
| title | Regulating NKX3.1 stability and function: Post-translational modifications and structural determinants |
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