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dc.contributor.authorAmlan, Das
dc.contributor.authorBase, Christine
dc.contributor.authorDhulipala, Srilakshmi
dc.contributor.authorDubreuil, Ronald R
dc.date.accessioned2011-01-09T22:06:12Z
dc.date.available2011-01-09T22:06:12Z
dc.date.issued2006-10-23
dc.identifier.bibliographicCitationDas, A., C. Base, S. Dhulipala, and R. R. Dubreuil, 2006, Spectrin functions upstream of ankyrin in a spectrin cytoskeleton assembly pathway: Journal of Cell Biology, v. 175, no. 2, p. 325-335. DOI: 10.1083/jcb.200602095en
dc.identifier.issn0021-9525
dc.identifier.otherDOI: 10.1083/jcb.200602095
dc.identifier.urihttp://hdl.handle.net/10027/7207
dc.description.abstractPrevailing models place spectrin downstream of ankyrin in a pathway of assembly and function in polarized cells. We used a transgene rescue strategy in Drosophila melanogaster to test contributions of four specific functional sites in beta spectrin to its assembly and function. (1) Removal of the pleckstrin homology domain blocked polarized spectrin assembly in midgut epithelial cells and was usually lethal. (2) A point mutation in the tetramer formation site, modeled after a hereditary elliptocytosis mutation in human erythrocyte spectrin, had no detectable effect on function. (3) Replacement of repetitive segments 4 - 11 of beta spectrin with repeats 2 - 9 of a spectrin abolished function but did not prevent polarized assembly. (4) Removal of the putative ankyrinbinding site had an unexpectedly mild phenotype with no detectable effect on spectrin targeting to the plasma membrane. The results suggest an alternate pathway in which spectrin directs ankyrin assembly and in which some important functions of spectrin are independent of ankyrin.en
dc.language.isoen_USen
dc.publisherRockefeller University Pressen
dc.subjectdrosophila beta-spectrimen
dc.subjectpleckstrin homology domainen
dc.subjectaxon initial segmentsen
dc.titleSpectrin functions upstream of ankyrin in a spectrin cytoskeleton assembly pathwayen
dc.typeArticleen


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