KLP38B: a mitotic kinesin-related protein that binds PP1
We have identified a new member of the kinesin superfamily in Drosophila, KLP38B (kinesin-like protein at 38B). KLP38B was isolated through its two-hybrid interaction with the catalytic subunit of type 1 serine/threonine phosphoprotein phosphatase (PP1). We demonstrate that recombinant KLP38B and PP...
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| Veröffentlicht in: | The Journal of cell biology 1997-07, Vol.138 (2), p.395-409 |
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| container_title | The Journal of cell biology |
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| creator | Alphey, L Parker, L Hawcroft, G Guo, Y.Q Kaiser, K Morgan, G |
| description | We have identified a new member of the kinesin superfamily in Drosophila, KLP38B (kinesin-like protein at 38B). KLP38B was isolated through its two-hybrid interaction with the catalytic subunit of type 1 serine/threonine phosphoprotein phosphatase (PP1). We demonstrate that recombinant KLP38B and PP1 associate in vitro. This is the first demonstration of direct binding of a kinesin-related protein to a regulatory enzyme. Though most closely related to the Unc-104 subfamily of kinesin-related proteins, KLP38B is expressed only in proliferating cells. KLP38B mutants show cell proliferation defects in many tissues. KLP38B is required for normal chromatin condensation as embryos from KLP38B mutant mothers have undercondensed chromatin at metaphase and anaphase. This is the first time that a kinesin-related protein has been shown to have such a role. Incomplete lethality of a strong KLP38B allele suggests partial redundancy with one or more additional kinesin-related proteins. |
| doi_str_mv | 10.1083/jcb.138.2.395 |
| format | Article |
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KLP38B was isolated through its two-hybrid interaction with the catalytic subunit of type 1 serine/threonine phosphoprotein phosphatase (PP1). We demonstrate that recombinant KLP38B and PP1 associate in vitro. This is the first demonstration of direct binding of a kinesin-related protein to a regulatory enzyme. Though most closely related to the Unc-104 subfamily of kinesin-related proteins, KLP38B is expressed only in proliferating cells. KLP38B mutants show cell proliferation defects in many tissues. KLP38B is required for normal chromatin condensation as embryos from KLP38B mutant mothers have undercondensed chromatin at metaphase and anaphase. This is the first time that a kinesin-related protein has been shown to have such a role. Incomplete lethality of a strong KLP38B allele suggests partial redundancy with one or more additional kinesin-related proteins.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.138.2.395</identifier><identifier>PMID: 9230081</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Animals ; Base Sequence ; binding ; binding proteins ; Cell Cycle ; Cell Division ; Cells ; Cellular biology ; Chromatin ; chromatin condensation ; chromosome mapping ; Chromosomes ; Cloning, Molecular ; Complementary DNA ; DNA, Complementary - genetics ; Drosophila ; Drosophila - enzymology ; Drosophila - genetics ; Drosophila melanogaster ; Drosophila Proteins ; Embryos ; Female ; female fertility ; Fertility ; follicles ; genbank/x99617 ; gene expression ; Gene Expression Regulation, Enzymologic ; Germ cells ; Insects ; Kinesins - genetics ; Kinesins - metabolism ; Kinesins - physiology ; Male ; messenger RNA ; mitosis ; Mitosis - physiology ; Molecular Sequence Data ; mutants ; Mutation ; Neurons ; nucleotide sequences ; Organ Specificity ; Phenotypes ; phosphoprotein phosphatase ; Phosphoprotein Phosphatases - metabolism ; Proteins ; Restriction Mapping ; RNA, Messenger - analysis ; Sequence Analysis, DNA ; Sequence Homology, Amino Acid ; transcription (genetics)</subject><ispartof>The Journal of cell biology, 1997-07, Vol.138 (2), p.395-409</ispartof><rights>Copyright 1997 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Jul 28, 1997</rights><rights>1997</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c485t-9e5e8a05cbdbdfa7f5e28fb7b1cc77950b805296dbf97554ad545a109664563a3</citedby><cites>FETCH-LOGICAL-c485t-9e5e8a05cbdbdfa7f5e28fb7b1cc77950b805296dbf97554ad545a109664563a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9230081$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Alphey, L</creatorcontrib><creatorcontrib>Parker, L</creatorcontrib><creatorcontrib>Hawcroft, G</creatorcontrib><creatorcontrib>Guo, Y.Q</creatorcontrib><creatorcontrib>Kaiser, K</creatorcontrib><creatorcontrib>Morgan, G</creatorcontrib><title>KLP38B: a mitotic kinesin-related protein that binds PP1</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>We have identified a new member of the kinesin superfamily in Drosophila, KLP38B (kinesin-like protein at 38B). KLP38B was isolated through its two-hybrid interaction with the catalytic subunit of type 1 serine/threonine phosphoprotein phosphatase (PP1). We demonstrate that recombinant KLP38B and PP1 associate in vitro. This is the first demonstration of direct binding of a kinesin-related protein to a regulatory enzyme. Though most closely related to the Unc-104 subfamily of kinesin-related proteins, KLP38B is expressed only in proliferating cells. KLP38B mutants show cell proliferation defects in many tissues. KLP38B is required for normal chromatin condensation as embryos from KLP38B mutant mothers have undercondensed chromatin at metaphase and anaphase. This is the first time that a kinesin-related protein has been shown to have such a role. Incomplete lethality of a strong KLP38B allele suggests partial redundancy with one or more additional kinesin-related proteins.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>binding</subject><subject>binding proteins</subject><subject>Cell Cycle</subject><subject>Cell Division</subject><subject>Cells</subject><subject>Cellular biology</subject><subject>Chromatin</subject><subject>chromatin condensation</subject><subject>chromosome mapping</subject><subject>Chromosomes</subject><subject>Cloning, Molecular</subject><subject>Complementary DNA</subject><subject>DNA, Complementary - genetics</subject><subject>Drosophila</subject><subject>Drosophila - enzymology</subject><subject>Drosophila - genetics</subject><subject>Drosophila melanogaster</subject><subject>Drosophila Proteins</subject><subject>Embryos</subject><subject>Female</subject><subject>female fertility</subject><subject>Fertility</subject><subject>follicles</subject><subject>genbank/x99617</subject><subject>gene expression</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Germ cells</subject><subject>Insects</subject><subject>Kinesins - genetics</subject><subject>Kinesins - metabolism</subject><subject>Kinesins - physiology</subject><subject>Male</subject><subject>messenger RNA</subject><subject>mitosis</subject><subject>Mitosis - physiology</subject><subject>Molecular Sequence Data</subject><subject>mutants</subject><subject>Mutation</subject><subject>Neurons</subject><subject>nucleotide sequences</subject><subject>Organ Specificity</subject><subject>Phenotypes</subject><subject>phosphoprotein phosphatase</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Proteins</subject><subject>Restriction Mapping</subject><subject>RNA, Messenger - analysis</subject><subject>Sequence Analysis, DNA</subject><subject>Sequence Homology, Amino Acid</subject><subject>transcription (genetics)</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1vEzEQxS0EKmnhyA3EqgduG2b87R6QoOJLRCIS9Gx5d72tw2YdbAeJ_x5XicrHhdMc3k9vZt4j5AnCEkGzl5u-WyLTS7pkRtwjCxQcWo0c7pMFAMXWCCoektOcNwDAFWcn5MRQBqBxQfSn1ZrpNxeNa7ahxBL65luYfQ5zm_zkih-aXYrFh7kpN640XZiH3KzX-Ig8GN2U_ePjPCNX795-vfzQrj6__3j5etX2XIvSGi-8diD6buiG0alReKrHTnXY90oZAZ0GQY0cutEoIbgbBBcOwUjJhWSOnZFXB9_dvtv6ofdzSW6yuxS2Lv200QX7tzKHG3sdf1haQ0GD1eDF0SDF73ufi92G3PtpcrOP-2yVQS5Rwn9BlJRTIVUFz_8BN3Gf5ppCXapAMU1ZhdoD1KeYc_Lj3ckI9rY4W4uz9UZLbS2u8s_-_POOPjZV9acHfZNLTL_NJGoUt-ueH-TRReuuU8j26gsFZEC1MlwK9gut6KSl</recordid><startdate>19970728</startdate><enddate>19970728</enddate><creator>Alphey, L</creator><creator>Parker, L</creator><creator>Hawcroft, G</creator><creator>Guo, Y.Q</creator><creator>Kaiser, K</creator><creator>Morgan, G</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</general><scope>FBQ</scope><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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7SS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19970728</creationdate><title>KLP38B: a mitotic kinesin-related protein that binds PP1</title><author>Alphey, L ; Parker, L ; Hawcroft, G ; Guo, Y.Q ; Kaiser, K ; Morgan, G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c485t-9e5e8a05cbdbdfa7f5e28fb7b1cc77950b805296dbf97554ad545a109664563a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>binding</topic><topic>binding proteins</topic><topic>Cell Cycle</topic><topic>Cell Division</topic><topic>Cells</topic><topic>Cellular biology</topic><topic>Chromatin</topic><topic>chromatin condensation</topic><topic>chromosome mapping</topic><topic>Chromosomes</topic><topic>Cloning, Molecular</topic><topic>Complementary DNA</topic><topic>DNA, Complementary - genetics</topic><topic>Drosophila</topic><topic>Drosophila - enzymology</topic><topic>Drosophila - genetics</topic><topic>Drosophila melanogaster</topic><topic>Drosophila Proteins</topic><topic>Embryos</topic><topic>Female</topic><topic>female fertility</topic><topic>Fertility</topic><topic>follicles</topic><topic>genbank/x99617</topic><topic>gene expression</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Germ cells</topic><topic>Insects</topic><topic>Kinesins - genetics</topic><topic>Kinesins - metabolism</topic><topic>Kinesins - physiology</topic><topic>Male</topic><topic>messenger RNA</topic><topic>mitosis</topic><topic>Mitosis - physiology</topic><topic>Molecular Sequence Data</topic><topic>mutants</topic><topic>Mutation</topic><topic>Neurons</topic><topic>nucleotide sequences</topic><topic>Organ Specificity</topic><topic>Phenotypes</topic><topic>phosphoprotein phosphatase</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Proteins</topic><topic>Restriction Mapping</topic><topic>RNA, Messenger - analysis</topic><topic>Sequence Analysis, DNA</topic><topic>Sequence Homology, Amino Acid</topic><topic>transcription (genetics)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Alphey, L</creatorcontrib><creatorcontrib>Parker, L</creatorcontrib><creatorcontrib>Hawcroft, G</creatorcontrib><creatorcontrib>Guo, Y.Q</creatorcontrib><creatorcontrib>Kaiser, K</creatorcontrib><creatorcontrib>Morgan, G</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Alphey, L</au><au>Parker, L</au><au>Hawcroft, G</au><au>Guo, Y.Q</au><au>Kaiser, K</au><au>Morgan, G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>KLP38B: a mitotic kinesin-related protein that binds PP1</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1997-07-28</date><risdate>1997</risdate><volume>138</volume><issue>2</issue><spage>395</spage><epage>409</epage><pages>395-409</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>We have identified a new member of the kinesin superfamily in Drosophila, KLP38B (kinesin-like protein at 38B). KLP38B was isolated through its two-hybrid interaction with the catalytic subunit of type 1 serine/threonine phosphoprotein phosphatase (PP1). We demonstrate that recombinant KLP38B and PP1 associate in vitro. This is the first demonstration of direct binding of a kinesin-related protein to a regulatory enzyme. Though most closely related to the Unc-104 subfamily of kinesin-related proteins, KLP38B is expressed only in proliferating cells. KLP38B mutants show cell proliferation defects in many tissues. KLP38B is required for normal chromatin condensation as embryos from KLP38B mutant mothers have undercondensed chromatin at metaphase and anaphase. This is the first time that a kinesin-related protein has been shown to have such a role. Incomplete lethality of a strong KLP38B allele suggests partial redundancy with one or more additional kinesin-related proteins.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>9230081</pmid><doi>10.1083/jcb.138.2.395</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of cell biology, 1997-07, Vol.138 (2), p.395-409 |
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| subjects | Amino Acid Sequence amino acid sequences Animals Base Sequence binding binding proteins Cell Cycle Cell Division Cells Cellular biology Chromatin chromatin condensation chromosome mapping Chromosomes Cloning, Molecular Complementary DNA DNA, Complementary - genetics Drosophila Drosophila - enzymology Drosophila - genetics Drosophila melanogaster Drosophila Proteins Embryos Female female fertility Fertility follicles genbank/x99617 gene expression Gene Expression Regulation, Enzymologic Germ cells Insects Kinesins - genetics Kinesins - metabolism Kinesins - physiology Male messenger RNA mitosis Mitosis - physiology Molecular Sequence Data mutants Mutation Neurons nucleotide sequences Organ Specificity Phenotypes phosphoprotein phosphatase Phosphoprotein Phosphatases - metabolism Proteins Restriction Mapping RNA, Messenger - analysis Sequence Analysis, DNA Sequence Homology, Amino Acid transcription (genetics) |
| title | KLP38B: a mitotic kinesin-related protein that binds PP1 |
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