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The M3 phosphorylation motif has been functionally conserved for intracellular trafficking of long-looped PIN-FORMEDs in the Arabidopsis root hair cell

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dc.contributor.authorSasayama, Daisuke-
dc.contributor.authorGanguly, Anindya-
dc.contributor.authorPark, Minho-
dc.contributor.authorCho, Hyung-Taeg-
dc.date.accessioned2014-04-03T01:05:54Z-
dc.date.available2014-04-03T01:05:54Z-
dc.date.issued2013-11-26-
dc.identifier.citationBMC Plant Biology Vol. 13 No.1, pp.1-11ko_KR
dc.identifier.issn1471-2229-
dc.identifier.urihttps://hdl.handle.net/10371/91315-
dc.description.abstractBackground : PIN-FORMED (PIN) efflux carriers contribute to polar auxin transport and plant development by exhibiting dynamic and diverse asymmetrical localization patterns in the plasma membrane (PM). Phosphorylation of the central hydrophilic loop (HL) of PINs has been implicated in the regulation of PIN trafficking. Recently, we reported that a phosphorylatable motif (M3) in the PIN3-HL is necessary for the polarity, intracellular trafficking, and biological functions of PIN3. In this study, using the root hair system for PIN activity assay, we investigated whether this motif has been functionally conserved among long-HL PINs.

Results : Root hair-specific overexpression of wild-type PIN1, 2, or 7 greatly inhibited root hair growth by depleting auxin levels in the root hair cell, whereas overexpression of M3 phosphorylation-defective PIN mutants failed to inhibit root hair growth. Consistent with this root hair phenotype, the PM localization of M3 phosphorylation-defective PIN1 and PIN7 was partially disrupted, resulting in less auxin efflux and restoration of root hair growth. Partial formation of brefeldin A-compartments in these phosphorylation-mutant PIN lines also suggested that their PM targeting was partially disrupted. On the other hand, compared with the PIN1 and PIN7 mutant proteins, M3-phosphorylation-defective PIN2 proteins were almost undetectable. However, the mutant PIN2 protein levels were restored by wortmannin treatment almost to the wild-type PIN2 level, indicating that the M3 motif of PIN2, unlike that of other PINs, is implicated in PIN2 trafficking to the vacuolar lytic pathway.
Conclusions : These results suggest that the M3 phosphorylation motif has been functionally conserved to modulate the intracellular trafficking of long-HL PINs, but its specific function in trafficking has diverged among PIN members.
ko_KR
dc.description.sponsorshipThis work was supported by grants from the Mid-career Researcher Program (2011–0017242, NRF, MEST) and the Next-Generation BioGreen 21 programs (TAGC PJ00820701 and SSAC PJ00951404) of the Rural Development Administration.ko_KR
dc.language.isoenko_KR
dc.publisherBioMed Central Ltd.ko_KR
dc.subjectAuxinko_KR
dc.subjectAuxin transportko_KR
dc.subjectHydrophilic loop (of PINs)ko_KR
dc.subjectPhosphorylationko_KR
dc.subjectPIN-FORMED (PIN)ko_KR
dc.subjectProtein traffickingko_KR
dc.subjectRoot hairko_KR
dc.titleThe M3 phosphorylation motif has been functionally conserved for intracellular trafficking of long-looped PIN-FORMEDs in the Arabidopsis root hair cellko_KR
dc.typeArticleko_KR
dc.contributor.AlternativeAuthor박민호-
dc.contributor.AlternativeAuthor조형택-
dc.identifier.doi10.1186/1471-2229-13-189-
dc.citation.journaltitleBMC Plant Biology-
dc.language.rfc3066en-
dc.description.versionPeer Reviewed-
dc.rights.holderDaisuke Sasayama et al.; licensee BioMed Central Ltd.-
dc.date.updated2014-04-02T14:21:33Z-
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College of Natural Sciences (자연과학대학)Dept. of Biological Sciences (생명과학부)Journal Papers (저널논문_생명과학부)
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