Arabidopsis KCBP interacts with AIR9 but stays in the cortical division zone throughout mitosis via its MyTH4-FERM domain
DC Element | Wert | Sprache |
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dc.contributor.author | Buschmann, Henrik | |
dc.contributor.author | Dols, Jacqueline | |
dc.contributor.author | Kopischke, Sarah | |
dc.contributor.author | Pena, Eduardo J. | |
dc.contributor.author | Andrade-Navarro, Miguel A. | |
dc.contributor.author | Heinlein, Manfred | |
dc.contributor.author | Szymanski, Daniel B. | |
dc.contributor.author | Zachgo, Sabine | |
dc.contributor.author | Doonan, John H. | |
dc.contributor.author | Lloyd, Clive W. | |
dc.date.accessioned | 2021-12-23T16:23:44Z | - |
dc.date.available | 2021-12-23T16:23:44Z | - |
dc.date.issued | 2015 | |
dc.identifier.issn | 00219533 | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/14642 | - |
dc.description.abstract | The preprophase band of microtubules performs the crucial function of marking the plane of cell division. Although the preprophase band depolymerises at the onset of mitosis, the division plane is `memorized' by a cortical division zone to which the phragmoplast is attracted during cytokinesis. Proteins have been discovered that are part of the molecular memory but little is known about how they contribute to phragmoplast guidance. Previously, we found that the microtubule-associated protein AIR9 is found in the cortical division zone at preprophase and returns during cell plate insertion but is absent from the cortex during the intervening mitosis. To identify new components of the preprophase memory, we searched for proteins that interact with AIR9. We detected the kinesin-like calmodulin-binding protein, KCBP, which can be visualized at the predicted cortical site throughout division. A truncation study of KCBP indicates that its MyTH4-FERM domain is required for linking the motor domain to the cortex. These results suggest a mechanism by which minus-end-directed KCBP helps guide the centrifugally expanding phragmoplast to the cortical division site. | |
dc.description.sponsorship | Biotechnology and Biological Sciences Research Council (BBSRC)UK Research & Innovation (UKRI)Biotechnology and Biological Sciences Research Council (BBSRC) [BB/E022634/1]; EMBO short-term fellowshipEuropean Molecular Biology Organization (EMBO) [ASTF 169.00-2011]; Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [ZA 259/6]; Leonardo Da Vinci programme of the European Union; Biotechnology and Biological Sciences Research CouncilUK Research & Innovation (UKRI)Biotechnology and Biological Sciences Research Council (BBSRC) [BB/D52189X/1, BB/E022634/1] Funding Source: researchfish; BBSRCUK Research & Innovation (UKRI)Biotechnology and Biological Sciences Research Council (BBSRC) [BB/E022634/1, BB/D52189X/1] Funding Source: UKRI; This work was supported by the Biotechnology and Biological Sciences Research Council (BBSRC) [grant number BB/E022634/1 to C.W.L. and J.H.D.]; by an EMBO short-term fellowship [grant number ASTF 169.00-2011 to H.B.]; and by Deutsche Forschungsgemeinschaft [grant number ZA 259/6 to S.Z.]. J.D. was supported by the Leonardo Da Vinci programme of the European Union. | |
dc.language.iso | en | |
dc.publisher | COMPANY BIOLOGISTS LTD | |
dc.relation.ispartof | JOURNAL OF CELL SCIENCE | |
dc.subject | AIR9 | |
dc.subject | Arabidopsis | |
dc.subject | CALMODULIN-BINDING PROTEIN | |
dc.subject | Cell Biology | |
dc.subject | Cell division | |
dc.subject | CULTURED TOBACCO CELLS | |
dc.subject | CYTOKINETIC APPARATUS | |
dc.subject | F-ACTIN | |
dc.subject | IN-SITU HYBRIDIZATION | |
dc.subject | Kinesin | |
dc.subject | MyTH4-FERM | |
dc.subject | PLANT-CELLS | |
dc.subject | PREPROPHASE BAND | |
dc.subject | SOMATIC CYTOKINESIS | |
dc.subject | SPATIAL CONTROL | |
dc.subject | TRICHOME MORPHOGENESIS | |
dc.title | Arabidopsis KCBP interacts with AIR9 but stays in the cortical division zone throughout mitosis via its MyTH4-FERM domain | |
dc.type | journal article | |
dc.identifier.doi | 10.1242/jcs.156570 | |
dc.identifier.isi | ISI:000355559600004 | |
dc.description.volume | 128 | |
dc.description.issue | 11 | |
dc.description.startpage | 2033 | |
dc.description.endpage | 2046 | |
dc.contributor.orcid | 0000-0001-6027-1919 | |
dc.identifier.eissn | 14779137 | |
dc.publisher.place | BIDDER BUILDING, STATION RD, HISTON, CAMBRIDGE CB24 9LF, ENGLAND | |
dcterms.isPartOf.abbreviation | J. Cell Sci. | |
dcterms.oaStatus | Green Published, Bronze | |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.dept | FB 05 - Biologie/Chemie | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.deptid | fb05 | - |
crisitem.author.orcid | 0000-0003-3022-6150 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | BuHe301 | - |
crisitem.author.netid | ZaSa518 | - |
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