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MIB-1 Is Required for Spermatogenesis and Facilitates LIN-12 and GLP-1 Activity in Caenorhabditis elegans
Covalent attachment of ubiquitin to substrate proteins changes their function or marks them for proteolysis, and the specificity of ubiquitin attachment is mediated by the numerous E3 ligases encoded by animals. Mind Bomb is an essential E3 ligase during Notch pathway signaling in insects and verteb...
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| Published in: | Genetics (Austin) 2018-05, Vol.209 (1), p.173-193 |
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| creator | Ratliff, Miriam Hill-Harfe, Katherine L Gleason, Elizabeth J Ling, Huiping Kroft, Tim L L'Hernault, Steven W |
| description | Covalent attachment of ubiquitin to substrate proteins changes their function or marks them for proteolysis, and the specificity of ubiquitin attachment is mediated by the numerous E3 ligases encoded by animals. Mind Bomb is an essential E3 ligase during Notch pathway signaling in insects and vertebrates. While
encodes a Mind Bomb homolog (
), it has never been recovered in the extensive Notch suppressor/enhancer screens that have identified numerous pathway components. Here, we show that
null mutants have a spermatogenesis-defective phenotype that results in a heterogeneous mixture of arrested spermatocytes, defective spermatids, and motility-impaired spermatozoa.
mutants also have chromosome segregation defects during meiosis, molecular null mutants are intrinsically temperature-sensitive, and many
spermatids contain large amounts of tubulin. These phenotypic features are similar to the endogenous RNA intereference (RNAi) mutants, but
mutants do not affect RNAi. MIB-1 protein is expressed throughout the germ line with peak expression in spermatocytes followed by segregation into the residual body during spermatid formation.
expression, while upregulated during spermatogenesis, also occurs somatically, including in vulva precursor cells. Here, we show that
mutants suppress both
and
(
Notch) gain-of-function mutants, restoring anchor cell formation and a functional vulva to the former and partly restoring oocyte production to the latter. However, suppressed hermaphrodites are only observed when grown at 25°, and they are self-sterile. This probably explains why
was not previously recovered as a Notch pathway component in suppressor/enhancer selection experiments. |
| doi_str_mv | 10.1534/genetics.118.300807 |
| format | article |
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encodes a Mind Bomb homolog (
), it has never been recovered in the extensive Notch suppressor/enhancer screens that have identified numerous pathway components. Here, we show that
null mutants have a spermatogenesis-defective phenotype that results in a heterogeneous mixture of arrested spermatocytes, defective spermatids, and motility-impaired spermatozoa.
mutants also have chromosome segregation defects during meiosis, molecular null mutants are intrinsically temperature-sensitive, and many
spermatids contain large amounts of tubulin. These phenotypic features are similar to the endogenous RNA intereference (RNAi) mutants, but
mutants do not affect RNAi. MIB-1 protein is expressed throughout the germ line with peak expression in spermatocytes followed by segregation into the residual body during spermatid formation.
expression, while upregulated during spermatogenesis, also occurs somatically, including in vulva precursor cells. Here, we show that
mutants suppress both
and
(
Notch) gain-of-function mutants, restoring anchor cell formation and a functional vulva to the former and partly restoring oocyte production to the latter. However, suppressed hermaphrodites are only observed when grown at 25°, and they are self-sterile. This probably explains why
was not previously recovered as a Notch pathway component in suppressor/enhancer selection experiments.</description><identifier>ISSN: 1943-2631</identifier><identifier>ISSN: 0016-6731</identifier><identifier>EISSN: 1943-2631</identifier><identifier>DOI: 10.1534/genetics.118.300807</identifier><identifier>PMID: 29531012</identifier><language>eng</language><publisher>United States: Genetics Society of America</publisher><subject>2-Methylisoborneol ; Alleles ; Animals ; Caenorhabditis elegans ; Caenorhabditis elegans - genetics ; Caenorhabditis elegans - metabolism ; Caenorhabditis elegans Proteins - genetics ; Caenorhabditis elegans Proteins - metabolism ; Coding ; Drosophila ; Gene expression ; Gene Expression Regulation, Developmental ; Genetics ; Glucagon-Like Peptide 1 - metabolism ; Hermaphrodites ; Homology ; Insects ; Investigations ; Kinases ; LIN-12 protein ; Loss of Function Mutation ; Meiosis ; Molecular chains ; Mutants ; Mutation ; Nematodes ; Notch protein ; Phenotype ; Phenotypes ; Proteins ; Proteolysis ; Receptors, Notch - metabolism ; Ribonucleic acid ; RNA ; RNA-mediated interference ; Screens ; Signal Transduction ; Spermatids ; Spermatocytes ; Spermatogenesis ; Spermatogenesis - genetics ; Spermatozoa ; Substrates ; Tubulin ; Ubiquitin ; Ubiquitin-protein ligase ; Ubiquitin-Protein Ligases - genetics ; Ubiquitin-Protein Ligases - metabolism ; Vertebrates ; Viral infections ; Vulva ; Worms</subject><ispartof>Genetics (Austin), 2018-05, Vol.209 (1), p.173-193</ispartof><rights>Copyright © 2018 by the Genetics Society of America.</rights><rights>Copyright Genetics Society of America May 2018</rights><rights>Copyright © 2018 by the Genetics Society of America 2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c433t-b6c78f63900ce2896cd77542407e57442f9325e57d1f165a890a9010ba7b1dde3</citedby><cites>FETCH-LOGICAL-c433t-b6c78f63900ce2896cd77542407e57442f9325e57d1f165a890a9010ba7b1dde3</cites><orcidid>0000-0002-1597-1008</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,315,786,790,891,27957,27958</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29531012$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ratliff, Miriam</creatorcontrib><creatorcontrib>Hill-Harfe, Katherine L</creatorcontrib><creatorcontrib>Gleason, Elizabeth J</creatorcontrib><creatorcontrib>Ling, Huiping</creatorcontrib><creatorcontrib>Kroft, Tim L</creatorcontrib><creatorcontrib>L'Hernault, Steven W</creatorcontrib><title>MIB-1 Is Required for Spermatogenesis and Facilitates LIN-12 and GLP-1 Activity in Caenorhabditis elegans</title><title>Genetics (Austin)</title><addtitle>Genetics</addtitle><description>Covalent attachment of ubiquitin to substrate proteins changes their function or marks them for proteolysis, and the specificity of ubiquitin attachment is mediated by the numerous E3 ligases encoded by animals. Mind Bomb is an essential E3 ligase during Notch pathway signaling in insects and vertebrates. While
encodes a Mind Bomb homolog (
), it has never been recovered in the extensive Notch suppressor/enhancer screens that have identified numerous pathway components. Here, we show that
null mutants have a spermatogenesis-defective phenotype that results in a heterogeneous mixture of arrested spermatocytes, defective spermatids, and motility-impaired spermatozoa.
mutants also have chromosome segregation defects during meiosis, molecular null mutants are intrinsically temperature-sensitive, and many
spermatids contain large amounts of tubulin. These phenotypic features are similar to the endogenous RNA intereference (RNAi) mutants, but
mutants do not affect RNAi. MIB-1 protein is expressed throughout the germ line with peak expression in spermatocytes followed by segregation into the residual body during spermatid formation.
expression, while upregulated during spermatogenesis, also occurs somatically, including in vulva precursor cells. Here, we show that
mutants suppress both
and
(
Notch) gain-of-function mutants, restoring anchor cell formation and a functional vulva to the former and partly restoring oocyte production to the latter. However, suppressed hermaphrodites are only observed when grown at 25°, and they are self-sterile. This probably explains why
was not previously recovered as a Notch pathway component in suppressor/enhancer selection experiments.</description><subject>2-Methylisoborneol</subject><subject>Alleles</subject><subject>Animals</subject><subject>Caenorhabditis elegans</subject><subject>Caenorhabditis elegans - genetics</subject><subject>Caenorhabditis elegans - metabolism</subject><subject>Caenorhabditis elegans Proteins - genetics</subject><subject>Caenorhabditis elegans Proteins - metabolism</subject><subject>Coding</subject><subject>Drosophila</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Genetics</subject><subject>Glucagon-Like Peptide 1 - metabolism</subject><subject>Hermaphrodites</subject><subject>Homology</subject><subject>Insects</subject><subject>Investigations</subject><subject>Kinases</subject><subject>LIN-12 protein</subject><subject>Loss of Function Mutation</subject><subject>Meiosis</subject><subject>Molecular chains</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Nematodes</subject><subject>Notch protein</subject><subject>Phenotype</subject><subject>Phenotypes</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Receptors, Notch - metabolism</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA-mediated interference</subject><subject>Screens</subject><subject>Signal Transduction</subject><subject>Spermatids</subject><subject>Spermatocytes</subject><subject>Spermatogenesis</subject><subject>Spermatogenesis - genetics</subject><subject>Spermatozoa</subject><subject>Substrates</subject><subject>Tubulin</subject><subject>Ubiquitin</subject><subject>Ubiquitin-protein ligase</subject><subject>Ubiquitin-Protein Ligases - genetics</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><subject>Vertebrates</subject><subject>Viral infections</subject><subject>Vulva</subject><subject>Worms</subject><issn>1943-2631</issn><issn>0016-6731</issn><issn>1943-2631</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNpdkVtv1DAQhS1ERUvhFyChSLzwkmV8S-IXpLJqy0pbQFyeLceZbF1l7a3tVOq_r8u2VeFpRuPvnPHoEPKOwoJKLj5t0GN2Ni0o7RYcoIP2BTmiSvCaNZy-fNYfktcpXQFAo2T3ihwyJTkFyo6Iu1h9qWm1StVPvJ5dxKEaQ6x-7TBuTQ73O5JLlfFDdWasm1w2GVO1Xn2rKfs7Pl__KAYnNrsbl28r56ulQR_ipekHl4sWJ9wYn96Qg9FMCd8-1GPy5-z09_Jrvf5-vlqerGsrOM9139i2GxuuACyyTjV2aFspmIAWZSsEGxVnsrQDHWkjTafAKKDQm7anw4D8mHze--7mfouDRZ-jmfQuuq2JtzoYp_998e5Sb8KNlopL4FAMPj4YxHA9Y8p665LFaTIew5w0A8olA0ZVQT_8h16FOfpyXqEEawVjtCsU31M2hpQijk-foaDvo9SPUeoSpd5HWVTvn9_xpHnMjt8B31iahA</recordid><startdate>20180501</startdate><enddate>20180501</enddate><creator>Ratliff, Miriam</creator><creator>Hill-Harfe, Katherine L</creator><creator>Gleason, Elizabeth J</creator><creator>Ling, Huiping</creator><creator>Kroft, Tim L</creator><creator>L'Hernault, Steven W</creator><general>Genetics Society of America</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>4T-</scope><scope>4U-</scope><scope>7QP</scope><scope>7SS</scope><scope>7TK</scope><scope>7TM</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>HCIFZ</scope><scope>K9-</scope><scope>K9.</scope><scope>LK8</scope><scope>M0K</scope><scope>M0R</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-1597-1008</orcidid></search><sort><creationdate>20180501</creationdate><title>MIB-1 Is Required for Spermatogenesis and Facilitates LIN-12 and GLP-1 Activity in Caenorhabditis elegans</title><author>Ratliff, Miriam ; Hill-Harfe, Katherine L ; Gleason, Elizabeth J ; Ling, Huiping ; Kroft, Tim L ; L'Hernault, Steven W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c433t-b6c78f63900ce2896cd77542407e57442f9325e57d1f165a890a9010ba7b1dde3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>2-Methylisoborneol</topic><topic>Alleles</topic><topic>Animals</topic><topic>Caenorhabditis elegans</topic><topic>Caenorhabditis elegans - genetics</topic><topic>Caenorhabditis elegans - metabolism</topic><topic>Caenorhabditis elegans Proteins - genetics</topic><topic>Caenorhabditis elegans Proteins - metabolism</topic><topic>Coding</topic><topic>Drosophila</topic><topic>Gene expression</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Genetics</topic><topic>Glucagon-Like Peptide 1 - metabolism</topic><topic>Hermaphrodites</topic><topic>Homology</topic><topic>Insects</topic><topic>Investigations</topic><topic>Kinases</topic><topic>LIN-12 protein</topic><topic>Loss of Function Mutation</topic><topic>Meiosis</topic><topic>Molecular chains</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Nematodes</topic><topic>Notch protein</topic><topic>Phenotype</topic><topic>Phenotypes</topic><topic>Proteins</topic><topic>Proteolysis</topic><topic>Receptors, Notch - metabolism</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>RNA-mediated interference</topic><topic>Screens</topic><topic>Signal Transduction</topic><topic>Spermatids</topic><topic>Spermatocytes</topic><topic>Spermatogenesis</topic><topic>Spermatogenesis - genetics</topic><topic>Spermatozoa</topic><topic>Substrates</topic><topic>Tubulin</topic><topic>Ubiquitin</topic><topic>Ubiquitin-protein ligase</topic><topic>Ubiquitin-Protein Ligases - genetics</topic><topic>Ubiquitin-Protein Ligases - metabolism</topic><topic>Vertebrates</topic><topic>Viral infections</topic><topic>Vulva</topic><topic>Worms</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ratliff, Miriam</creatorcontrib><creatorcontrib>Hill-Harfe, Katherine L</creatorcontrib><creatorcontrib>Gleason, Elizabeth J</creatorcontrib><creatorcontrib>Ling, Huiping</creatorcontrib><creatorcontrib>Kroft, Tim L</creatorcontrib><creatorcontrib>L'Hernault, Steven W</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Docstoc</collection><collection>University Readers</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Agricultural Science Collection</collection><collection>ProQuest Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>ProQuest Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Agriculture & Environmental Science Database</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>Consumer Health Database (Alumni Edition)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Agriculture Science Database</collection><collection>ProQuest Consumer Health Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>ProQuest Research Library</collection><collection>ProQuest Science Journals</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Genetics (Austin)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ratliff, Miriam</au><au>Hill-Harfe, Katherine L</au><au>Gleason, Elizabeth J</au><au>Ling, Huiping</au><au>Kroft, Tim L</au><au>L'Hernault, Steven W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MIB-1 Is Required for Spermatogenesis and Facilitates LIN-12 and GLP-1 Activity in Caenorhabditis elegans</atitle><jtitle>Genetics (Austin)</jtitle><addtitle>Genetics</addtitle><date>2018-05-01</date><risdate>2018</risdate><volume>209</volume><issue>1</issue><spage>173</spage><epage>193</epage><pages>173-193</pages><issn>1943-2631</issn><issn>0016-6731</issn><eissn>1943-2631</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><notes>Present address: Department of Neurosurgery, University Medical Center Mannheim, University of Heidelberg, Theodor-Kutzer-Ufer 1-3, 68167 Mannheim, Germany.</notes><notes>Present address: Biology Department, Auburn University-Montgomery, Montgomery, AL 36117.</notes><abstract>Covalent attachment of ubiquitin to substrate proteins changes their function or marks them for proteolysis, and the specificity of ubiquitin attachment is mediated by the numerous E3 ligases encoded by animals. Mind Bomb is an essential E3 ligase during Notch pathway signaling in insects and vertebrates. While
encodes a Mind Bomb homolog (
), it has never been recovered in the extensive Notch suppressor/enhancer screens that have identified numerous pathway components. Here, we show that
null mutants have a spermatogenesis-defective phenotype that results in a heterogeneous mixture of arrested spermatocytes, defective spermatids, and motility-impaired spermatozoa.
mutants also have chromosome segregation defects during meiosis, molecular null mutants are intrinsically temperature-sensitive, and many
spermatids contain large amounts of tubulin. These phenotypic features are similar to the endogenous RNA intereference (RNAi) mutants, but
mutants do not affect RNAi. MIB-1 protein is expressed throughout the germ line with peak expression in spermatocytes followed by segregation into the residual body during spermatid formation.
expression, while upregulated during spermatogenesis, also occurs somatically, including in vulva precursor cells. Here, we show that
mutants suppress both
and
(
Notch) gain-of-function mutants, restoring anchor cell formation and a functional vulva to the former and partly restoring oocyte production to the latter. However, suppressed hermaphrodites are only observed when grown at 25°, and they are self-sterile. This probably explains why
was not previously recovered as a Notch pathway component in suppressor/enhancer selection experiments.</abstract><cop>United States</cop><pub>Genetics Society of America</pub><pmid>29531012</pmid><doi>10.1534/genetics.118.300807</doi><tpages>21</tpages><orcidid>https://orcid.org/0000-0002-1597-1008</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Genetics (Austin), 2018-05, Vol.209 (1), p.173-193 |
| issn | 1943-2631 0016-6731 1943-2631 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5935030 |
| source | Freely Accessible Science Journals - check A-Z of ejournals; Oxford Journals Online; Alma/SFX Local Collection |
| subjects | 2-Methylisoborneol Alleles Animals Caenorhabditis elegans Caenorhabditis elegans - genetics Caenorhabditis elegans - metabolism Caenorhabditis elegans Proteins - genetics Caenorhabditis elegans Proteins - metabolism Coding Drosophila Gene expression Gene Expression Regulation, Developmental Genetics Glucagon-Like Peptide 1 - metabolism Hermaphrodites Homology Insects Investigations Kinases LIN-12 protein Loss of Function Mutation Meiosis Molecular chains Mutants Mutation Nematodes Notch protein Phenotype Phenotypes Proteins Proteolysis Receptors, Notch - metabolism Ribonucleic acid RNA RNA-mediated interference Screens Signal Transduction Spermatids Spermatocytes Spermatogenesis Spermatogenesis - genetics Spermatozoa Substrates Tubulin Ubiquitin Ubiquitin-protein ligase Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism Vertebrates Viral infections Vulva Worms |
| title | MIB-1 Is Required for Spermatogenesis and Facilitates LIN-12 and GLP-1 Activity in Caenorhabditis elegans |
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