Arabidopsis KCBP interacts with AIR9 but stays in the cortical division zone throughout mitosis via its MyTH4-FERM domain

DC ElementWertSprache
dc.contributor.authorBuschmann, Henrik
dc.contributor.authorDols, Jacqueline
dc.contributor.authorKopischke, Sarah
dc.contributor.authorPena, Eduardo J.
dc.contributor.authorAndrade-Navarro, Miguel A.
dc.contributor.authorHeinlein, Manfred
dc.contributor.authorSzymanski, Daniel B.
dc.contributor.authorZachgo, Sabine
dc.contributor.authorDoonan, John H.
dc.contributor.authorLloyd, Clive W.
dc.date.accessioned2021-12-23T16:23:44Z-
dc.date.available2021-12-23T16:23:44Z-
dc.date.issued2015
dc.identifier.issn00219533
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/14642-
dc.description.abstractThe 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.sponsorshipBiotechnology 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.isoen
dc.publisherCOMPANY BIOLOGISTS LTD
dc.relation.ispartofJOURNAL OF CELL SCIENCE
dc.subjectAIR9
dc.subjectArabidopsis
dc.subjectCALMODULIN-BINDING PROTEIN
dc.subjectCell Biology
dc.subjectCell division
dc.subjectCULTURED TOBACCO CELLS
dc.subjectCYTOKINETIC APPARATUS
dc.subjectF-ACTIN
dc.subjectIN-SITU HYBRIDIZATION
dc.subjectKinesin
dc.subjectMyTH4-FERM
dc.subjectPLANT-CELLS
dc.subjectPREPROPHASE BAND
dc.subjectSOMATIC CYTOKINESIS
dc.subjectSPATIAL CONTROL
dc.subjectTRICHOME MORPHOGENESIS
dc.titleArabidopsis KCBP interacts with AIR9 but stays in the cortical division zone throughout mitosis via its MyTH4-FERM domain
dc.typejournal article
dc.identifier.doi10.1242/jcs.156570
dc.identifier.isiISI:000355559600004
dc.description.volume128
dc.description.issue11
dc.description.startpage2033
dc.description.endpage2046
dc.contributor.orcid0000-0001-6027-1919
dc.identifier.eissn14779137
dc.publisher.placeBIDDER BUILDING, STATION RD, HISTON, CAMBRIDGE CB24 9LF, ENGLAND
dcterms.isPartOf.abbreviationJ. Cell Sci.
dcterms.oaStatusGreen Published, Bronze
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0003-3022-6150-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidBuHe301-
crisitem.author.netidZaSa518-
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