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dc.contributor.authorCraige, Branch
dc.contributor.authorWitman, George B.
dc.date2022-08-11T08:08:03.000
dc.date.accessioned2022-08-23T15:40:42Z
dc.date.available2022-08-23T15:40:42Z
dc.date.issued2014-09-08
dc.date.submitted2015-04-01
dc.identifier.citationDev Cell. 2014 Sep 8;30(5):492-3. doi: 10.1016/j.devcel.2014.08.019. <a href="http://dx.doi.org/10.1016/j.devcel.2014.08.019">Link to article on publisher's site</a>
dc.identifier.issn1534-5807 (Linking)
dc.identifier.doi10.1016/j.devcel.2014.08.019
dc.identifier.pmid25203204
dc.identifier.urihttp://hdl.handle.net/20.500.14038/26461
dc.description.abstractCilia and flagella are assembled and maintained by the motor-driven, bidirectional traffic of large protein complexes in a process termed intraflagellar transport (IFT). In this issue of Developmental Cell, Liang et al. (2014) report that IFT is regulated in part by the phosphorylation status of the kinesin-II subunit FLA8/KIF3B.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=25203204&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4384660/
dc.subjectAnimals
dc.subjectCalcium-Binding Proteins
dc.subjectChlamydomonas reinhardtii
dc.subjectFlagella
dc.subject*Gene Expression Regulation, Plant
dc.subjectKinesin
dc.subjectCell and Developmental Biology
dc.subjectCell Biology
dc.subjectDevelopmental Biology
dc.titleFlipping a phosphate switch on kinesin-II to turn IFT around
dc.typeJournal Article
dc.source.journaltitleDevelopmental cell
dc.source.volume30
dc.source.issue5
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/cellbiology_pp/146
dc.identifier.contextkey6929796
html.description.abstract<p>Cilia and flagella are assembled and maintained by the motor-driven, bidirectional traffic of large protein complexes in a process termed intraflagellar transport (IFT). In this issue of Developmental Cell, Liang et al. (2014) report that IFT is regulated in part by the phosphorylation status of the kinesin-II subunit FLA8/KIF3B.</p>
dc.identifier.submissionpathcellbiology_pp/146
dc.contributor.departmentDepartment of Cell and Developmental Biology
dc.source.pages492-3


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