Nuclear Translocation of Extradenticle Requires homothorax, which Encodes an Extradenticle-Related Homeodomain Protein
We show that homothorax ( hth) is required for the Hox genes to pattern the body of the fruit fly, Drosophila melanogaster. hth is necessary for the nuclear localization of an essential HOX cofactor, Extradenticle (EXD), and encodes a homeodomain protein that shares extensive identity with the produ...
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Veröffentlicht in: | Cell 1997-10, Vol.91 (2), p.171-183 |
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creator | Rieckhof, Gabrielle E Casares, Fernando Ryoo, Hyung Don Abu-Shaar, Muna Mann, Richard S |
description | We show that
homothorax (
hth) is required for the
Hox genes to pattern the body of the fruit fly, Drosophila melanogaster.
hth is necessary for the nuclear localization of an essential HOX cofactor, Extradenticle (EXD), and encodes a homeodomain protein that shares extensive identity with the product of
Meis1, a murine proto-oncogene. MEIS1 is able to rescue
hth mutant phenotypes and can induce the cytoplasmic-to-nuclear translocation of EXD in cell culture and Drosophila embryos. Thus,
Meis1 is a murine homolog of
hth. MEIS1/HTH also specifically binds to EXD with high affinity in vitro. These data suggest a novel and evolutionarily conserved mechanism for regulating HOX activity in which a direct protein–protein interaction between EXD and HTH results in EXD's nuclear translocation. |
doi_str_mv | 10.1016/S0092-8674(00)80400-6 |
format | Article |
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homothorax (
hth) is required for the
Hox genes to pattern the body of the fruit fly, Drosophila melanogaster.
hth is necessary for the nuclear localization of an essential HOX cofactor, Extradenticle (EXD), and encodes a homeodomain protein that shares extensive identity with the product of
Meis1, a murine proto-oncogene. MEIS1 is able to rescue
hth mutant phenotypes and can induce the cytoplasmic-to-nuclear translocation of EXD in cell culture and Drosophila embryos. Thus,
Meis1 is a murine homolog of
hth. MEIS1/HTH also specifically binds to EXD with high affinity in vitro. These data suggest a novel and evolutionarily conserved mechanism for regulating HOX activity in which a direct protein–protein interaction between EXD and HTH results in EXD's nuclear translocation.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/S0092-8674(00)80400-6</identifier><identifier>PMID: 9346235</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animal Structures - physiology ; Animals ; Biological Transport - genetics ; Cell Nucleus - chemistry ; Cell Nucleus - metabolism ; Cytoplasm - chemistry ; DNA-Binding Proteins - analysis ; DNA-Binding Proteins - metabolism ; Drosophila melanogaster - genetics ; Drosophila Proteins ; Embryo, Nonmammalian - physiology ; Embryonic and Fetal Development - physiology ; Gene Expression Regulation, Developmental ; Genes, Homeobox - physiology ; Homeodomain Proteins - genetics ; Homeodomain Proteins - metabolism ; Leukemia, Myeloid ; Mice ; Molecular Sequence Data ; Myeloid Ecotropic Viral Integration Site 1 Protein ; Neoplasm Proteins - genetics ; Neoplasm Proteins - metabolism ; Sequence Homology, Amino Acid ; Transcription Factors - analysis ; Transcription Factors - metabolism</subject><ispartof>Cell, 1997-10, Vol.91 (2), p.171-183</ispartof><rights>1997 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c345t-a83c9313c428e7b0bd2afaf37d3d735885008825decacd31c5d5d03b91abf4c53</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0092-8674(00)80400-6$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9346235$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rieckhof, Gabrielle E</creatorcontrib><creatorcontrib>Casares, Fernando</creatorcontrib><creatorcontrib>Ryoo, Hyung Don</creatorcontrib><creatorcontrib>Abu-Shaar, Muna</creatorcontrib><creatorcontrib>Mann, Richard S</creatorcontrib><title>Nuclear Translocation of Extradenticle Requires homothorax, which Encodes an Extradenticle-Related Homeodomain Protein</title><title>Cell</title><addtitle>Cell</addtitle><description>We show that
homothorax (
hth) is required for the
Hox genes to pattern the body of the fruit fly, Drosophila melanogaster.
hth is necessary for the nuclear localization of an essential HOX cofactor, Extradenticle (EXD), and encodes a homeodomain protein that shares extensive identity with the product of
Meis1, a murine proto-oncogene. MEIS1 is able to rescue
hth mutant phenotypes and can induce the cytoplasmic-to-nuclear translocation of EXD in cell culture and Drosophila embryos. Thus,
Meis1 is a murine homolog of
hth. MEIS1/HTH also specifically binds to EXD with high affinity in vitro. These data suggest a novel and evolutionarily conserved mechanism for regulating HOX activity in which a direct protein–protein interaction between EXD and HTH results in EXD's nuclear translocation.</description><subject>Animal Structures - physiology</subject><subject>Animals</subject><subject>Biological Transport - genetics</subject><subject>Cell Nucleus - chemistry</subject><subject>Cell Nucleus - metabolism</subject><subject>Cytoplasm - chemistry</subject><subject>DNA-Binding Proteins - analysis</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Drosophila melanogaster - genetics</subject><subject>Drosophila Proteins</subject><subject>Embryo, Nonmammalian - physiology</subject><subject>Embryonic and Fetal Development - physiology</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Genes, Homeobox - physiology</subject><subject>Homeodomain Proteins - genetics</subject><subject>Homeodomain Proteins - metabolism</subject><subject>Leukemia, Myeloid</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Myeloid Ecotropic Viral Integration Site 1 Protein</subject><subject>Neoplasm Proteins - genetics</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Transcription Factors - analysis</subject><subject>Transcription Factors - metabolism</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkdFKHTEQhoNU9FT7CEKupIWunSSb3eyVFDmtBdGi9jpkk1lOym6iSdbq27vqodCrXs3F_83APx8hRwxOGLDmyw1AxyvVtPVHgE8KaoCq2SErBl1b1azl78jqL7JP3uf8GwCUlHKP7HWibriQK_JwOdsRTaK3yYQ8RmuKj4HGga4fSzIOQ_ELQK_xfvYJM93EKZZNTObxM_2z8XZD18FGtyQm_LtTXeNoCjp6HieMLk7GB_ozxYI-HJLdwYwZP2znAfn1bX17dl5dXH3_cfb1orKilqUySthOMGFrrrDtoXfcDGYQrROuFVIpuTRSXDq0xjrBrHTSgeg7ZvqhtlIckOO3u3cp3s-Yi558tjiOJmCcs2470YCs-X9B1nAOqlULeLQF535Cp--Sn0x60tuPLvnpW45LrQePSWfrMVh0y_ts0S56zUC_KNSvCvWLHw2gXxXqRjwDgeCPdg</recordid><startdate>19971017</startdate><enddate>19971017</enddate><creator>Rieckhof, Gabrielle E</creator><creator>Casares, Fernando</creator><creator>Ryoo, Hyung Don</creator><creator>Abu-Shaar, Muna</creator><creator>Mann, Richard S</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19971017</creationdate><title>Nuclear Translocation of Extradenticle Requires homothorax, which Encodes an Extradenticle-Related Homeodomain Protein</title><author>Rieckhof, Gabrielle E ; Casares, Fernando ; Ryoo, Hyung Don ; Abu-Shaar, Muna ; Mann, Richard S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c345t-a83c9313c428e7b0bd2afaf37d3d735885008825decacd31c5d5d03b91abf4c53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animal Structures - physiology</topic><topic>Animals</topic><topic>Biological Transport - genetics</topic><topic>Cell Nucleus - chemistry</topic><topic>Cell Nucleus - metabolism</topic><topic>Cytoplasm - chemistry</topic><topic>DNA-Binding Proteins - analysis</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Drosophila melanogaster - genetics</topic><topic>Drosophila Proteins</topic><topic>Embryo, Nonmammalian - physiology</topic><topic>Embryonic and Fetal Development - physiology</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Genes, Homeobox - physiology</topic><topic>Homeodomain Proteins - genetics</topic><topic>Homeodomain Proteins - metabolism</topic><topic>Leukemia, Myeloid</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Myeloid Ecotropic Viral Integration Site 1 Protein</topic><topic>Neoplasm Proteins - genetics</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Transcription Factors - analysis</topic><topic>Transcription Factors - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rieckhof, Gabrielle E</creatorcontrib><creatorcontrib>Casares, Fernando</creatorcontrib><creatorcontrib>Ryoo, Hyung Don</creatorcontrib><creatorcontrib>Abu-Shaar, Muna</creatorcontrib><creatorcontrib>Mann, Richard S</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rieckhof, Gabrielle E</au><au>Casares, Fernando</au><au>Ryoo, Hyung Don</au><au>Abu-Shaar, Muna</au><au>Mann, Richard S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nuclear Translocation of Extradenticle Requires homothorax, which Encodes an Extradenticle-Related Homeodomain Protein</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1997-10-17</date><risdate>1997</risdate><volume>91</volume><issue>2</issue><spage>171</spage><epage>183</epage><pages>171-183</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>We show that
homothorax (
hth) is required for the
Hox genes to pattern the body of the fruit fly, Drosophila melanogaster.
hth is necessary for the nuclear localization of an essential HOX cofactor, Extradenticle (EXD), and encodes a homeodomain protein that shares extensive identity with the product of
Meis1, a murine proto-oncogene. MEIS1 is able to rescue
hth mutant phenotypes and can induce the cytoplasmic-to-nuclear translocation of EXD in cell culture and Drosophila embryos. Thus,
Meis1 is a murine homolog of
hth. MEIS1/HTH also specifically binds to EXD with high affinity in vitro. These data suggest a novel and evolutionarily conserved mechanism for regulating HOX activity in which a direct protein–protein interaction between EXD and HTH results in EXD's nuclear translocation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9346235</pmid><doi>10.1016/S0092-8674(00)80400-6</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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source | MEDLINE; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; ScienceDirect Journals (5 years ago - present) |
subjects | Animal Structures - physiology Animals Biological Transport - genetics Cell Nucleus - chemistry Cell Nucleus - metabolism Cytoplasm - chemistry DNA-Binding Proteins - analysis DNA-Binding Proteins - metabolism Drosophila melanogaster - genetics Drosophila Proteins Embryo, Nonmammalian - physiology Embryonic and Fetal Development - physiology Gene Expression Regulation, Developmental Genes, Homeobox - physiology Homeodomain Proteins - genetics Homeodomain Proteins - metabolism Leukemia, Myeloid Mice Molecular Sequence Data Myeloid Ecotropic Viral Integration Site 1 Protein Neoplasm Proteins - genetics Neoplasm Proteins - metabolism Sequence Homology, Amino Acid Transcription Factors - analysis Transcription Factors - metabolism |
title | Nuclear Translocation of Extradenticle Requires homothorax, which Encodes an Extradenticle-Related Homeodomain Protein |
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