One of the protein phosphatase 1 isoenzymes in Drosophila is essential for mitosis
Drosophila has four loci encoding type 1 protein serine/threonine phosphatases (PP1s). Here we describe mutations in one of these genes, at 87B on chromosome 3. Mutants die at the larval-pupal boundary with little or no imaginal cell proliferation. Neuroblasts are delayed in progress through mitosis...
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| Veröffentlicht in: | Cell 1990-10, Vol.63 (1), p.33-46 |
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| creator | Axton, J.Myles Dombrádi, Vlktor Cohen, Patricia T.W. Glover, David M. |
| description | Drosophila has four loci encoding type 1 protein serine/threonine phosphatases (PP1s). Here we describe mutations in one of these genes, at 87B on chromosome 3. Mutants die at the larval-pupal boundary with little or no imaginal cell proliferation. Neuroblasts are delayed in progress through mitosis and show defective spindle organization, abnormal sister chromatid segregation, hyperploidy, and excessive chromosome condensation. Germline transformation of mutant files with the wild-type
PP1 87B gene restores normal mitosis, viability, and fertility. These results show that PP1 activity is required for mitotic progression and that the other loci cannot supply sufficient activity to complement loss of expression of the
PP1 87B gene. Alternatively, the
PP1 87B product may have a distinct specialized function in mitosis. |
| doi_str_mv | 10.1016/0092-8674(90)90286-N |
| format | Article |
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PP1 87B gene restores normal mitosis, viability, and fertility. These results show that PP1 activity is required for mitotic progression and that the other loci cannot supply sufficient activity to complement loss of expression of the
PP1 87B gene. Alternatively, the
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PP1 87B gene restores normal mitosis, viability, and fertility. These results show that PP1 activity is required for mitotic progression and that the other loci cannot supply sufficient activity to complement loss of expression of the
PP1 87B gene. Alternatively, the
PP1 87B product may have a distinct specialized function in mitosis.</description><subject>Alleles</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Chromosome Aberrations</subject><subject>Chromosome Mapping</subject><subject>Chromosomes - ultrastructure</subject><subject>DNA - genetics</subject><subject>DNA - isolation & purification</subject><subject>Drosophila</subject><subject>Drosophila - cytology</subject><subject>Drosophila - enzymology</subject><subject>Drosophila - genetics</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Female</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Hydrolases</topic><topic>Isoenzymes - genetics</topic><topic>Isoenzymes - metabolism</topic><topic>Male</topic><topic>Mitosis</topic><topic>Mutation</topic><topic>Neurons - cytology</topic><topic>Phosphoprotein Phosphatases - genetics</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Protein Phosphatase 1</topic><topic>Salivary Glands - cytology</topic><topic>Spindle Apparatus - ultrastructure</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Axton, J.Myles</creatorcontrib><creatorcontrib>Dombrádi, Vlktor</creatorcontrib><creatorcontrib>Cohen, Patricia T.W.</creatorcontrib><creatorcontrib>Glover, David M.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</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>Axton, J.Myles</au><au>Dombrádi, Vlktor</au><au>Cohen, Patricia T.W.</au><au>Glover, David M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>One of the protein phosphatase 1 isoenzymes in Drosophila is essential for mitosis</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1990-10-05</date><risdate>1990</risdate><volume>63</volume><issue>1</issue><spage>33</spage><epage>46</epage><pages>33-46</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><coden>CELLB5</coden><abstract>Drosophila has four loci encoding type 1 protein serine/threonine phosphatases (PP1s). Here we describe mutations in one of these genes, at 87B on chromosome 3. Mutants die at the larval-pupal boundary with little or no imaginal cell proliferation. Neuroblasts are delayed in progress through mitosis and show defective spindle organization, abnormal sister chromatid segregation, hyperploidy, and excessive chromosome condensation. Germline transformation of mutant files with the wild-type
PP1 87B gene restores normal mitosis, viability, and fertility. These results show that PP1 activity is required for mitotic progression and that the other loci cannot supply sufficient activity to complement loss of expression of the
PP1 87B gene. Alternatively, the
PP1 87B product may have a distinct specialized function in mitosis.</abstract><cop>Cambridge, MA</cop><pub>Elsevier Inc</pub><pmid>2170019</pmid><doi>10.1016/0092-8674(90)90286-N</doi><tpages>14</tpages></addata></record> |
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| subjects | Alleles Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Chromosome Aberrations Chromosome Mapping Chromosomes - ultrastructure DNA - genetics DNA - isolation & purification Drosophila Drosophila - cytology Drosophila - enzymology Drosophila - genetics Enzymes and enzyme inhibitors Female Fundamental and applied biological sciences. Psychology Hydrolases Isoenzymes - genetics Isoenzymes - metabolism Male Mitosis Mutation Neurons - cytology Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - metabolism Protein Phosphatase 1 Salivary Glands - cytology Spindle Apparatus - ultrastructure Transcription, Genetic |
| title | One of the protein phosphatase 1 isoenzymes in Drosophila is essential for mitosis |
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