Inactivation of plasma membrane-localized CDPK-RELATED KINASE5 decelerates PIN2 exocytosis and root gravitropic response in Arabidopsis

Gábor Rigó, F. Ayaydin, Olaf Tietz, Laura Zsigmond, Hajnalka Kovács, Anikó Páy, Klaus Salchert, Z. Darula, Katalin F. Medzihradszky, L. Szabados, Klaus Palme, Csaba Koncz, Ágnes Cséplo

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

CRK5 is a member of the Arabidopsis thaliana Ca2+/calmodulin-dependent kinase-related kinase family. Here, we show that inactivation of CRK5 inhibits primary root elongation and delays gravitropic bending of shoots and roots. Reduced activity of the auxin-induced DR5-green fluorescent protein reporter suggests that auxin is depleted from crk5 root tips. However, no tip collapse is observed and the transcription of genes for auxin biosynthesis, AUXIN TRANSPORTER/AUXIN TRANSPORTERLIKE PROTEIN (AUX/LAX) auxin influx, and PIN-FORMED (PIN) efflux carriers is unaffected by the crk5 mutation. Whereas AUX1, PIN1, PIN3, PIN4, and PIN7 display normal localization, PIN2 is depleted from apical membranes of epidermal cells and shows basal to apical relocalization in the cortex of the crk5 root transition zone. This, together with an increase in the number of crk5 lateral root primordia, suggests facilitated auxin efflux through the cortex toward the elongation zone. CRK5 is a plasma membrane-associated kinase that forms U-shaped patterns facing outer lateral walls of epidermis and cortex cells. Brefeldin inhibition of exocytosis stimulates CRK5 internalization into brefeldin bodies. CRK5 phosphorylates the hydrophilic loop of PIN2 in vitro, and PIN2 shows accelerated accumulation in brefeldin bodies in the crk5 mutant. Delayed gravitropic response of the crk5 mutant thus likely reflects defective phosphorylation of PIN2 and deceleration of its brefeldin-sensitive membrane recycling.

Original languageEnglish
Pages (from-to)1592-1608
Number of pages17
JournalPlant Cell
Volume25
Issue number5
DOIs
Publication statusPublished - May 2013

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Indoleacetic Acids
exocytosis
Exocytosis
Arabidopsis
auxins
inactivation
plasma membrane
Cell Membrane
cortex
phosphotransferases (kinases)
Phosphotransferases
root primordia
mutants
Calcium-Calmodulin-Dependent Protein Kinases
Meristem
Deceleration
calmodulin
epidermis (plant)
Green Fluorescent Proteins
green fluorescent protein

ASJC Scopus subject areas

  • Plant Science
  • Cell Biology

Cite this

Inactivation of plasma membrane-localized CDPK-RELATED KINASE5 decelerates PIN2 exocytosis and root gravitropic response in Arabidopsis. / Rigó, Gábor; Ayaydin, F.; Tietz, Olaf; Zsigmond, Laura; Kovács, Hajnalka; Páy, Anikó; Salchert, Klaus; Darula, Z.; Medzihradszky, Katalin F.; Szabados, L.; Palme, Klaus; Koncz, Csaba; Cséplo, Ágnes.

In: Plant Cell, Vol. 25, No. 5, 05.2013, p. 1592-1608.

Research output: Contribution to journalArticle

Rigó, G, Ayaydin, F, Tietz, O, Zsigmond, L, Kovács, H, Páy, A, Salchert, K, Darula, Z, Medzihradszky, KF, Szabados, L, Palme, K, Koncz, C & Cséplo, Á 2013, 'Inactivation of plasma membrane-localized CDPK-RELATED KINASE5 decelerates PIN2 exocytosis and root gravitropic response in Arabidopsis', Plant Cell, vol. 25, no. 5, pp. 1592-1608. https://doi.org/10.1105/tpc.113.110452
Rigó, Gábor ; Ayaydin, F. ; Tietz, Olaf ; Zsigmond, Laura ; Kovács, Hajnalka ; Páy, Anikó ; Salchert, Klaus ; Darula, Z. ; Medzihradszky, Katalin F. ; Szabados, L. ; Palme, Klaus ; Koncz, Csaba ; Cséplo, Ágnes. / Inactivation of plasma membrane-localized CDPK-RELATED KINASE5 decelerates PIN2 exocytosis and root gravitropic response in Arabidopsis. In: Plant Cell. 2013 ; Vol. 25, No. 5. pp. 1592-1608.
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AU - Zsigmond, Laura

AU - Kovács, Hajnalka

AU - Páy, Anikó

AU - Salchert, Klaus

AU - Darula, Z.

AU - Medzihradszky, Katalin F.

AU - Szabados, L.

AU - Palme, Klaus

AU - Koncz, Csaba

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N2 - CRK5 is a member of the Arabidopsis thaliana Ca2+/calmodulin-dependent kinase-related kinase family. Here, we show that inactivation of CRK5 inhibits primary root elongation and delays gravitropic bending of shoots and roots. Reduced activity of the auxin-induced DR5-green fluorescent protein reporter suggests that auxin is depleted from crk5 root tips. However, no tip collapse is observed and the transcription of genes for auxin biosynthesis, AUXIN TRANSPORTER/AUXIN TRANSPORTERLIKE PROTEIN (AUX/LAX) auxin influx, and PIN-FORMED (PIN) efflux carriers is unaffected by the crk5 mutation. Whereas AUX1, PIN1, PIN3, PIN4, and PIN7 display normal localization, PIN2 is depleted from apical membranes of epidermal cells and shows basal to apical relocalization in the cortex of the crk5 root transition zone. This, together with an increase in the number of crk5 lateral root primordia, suggests facilitated auxin efflux through the cortex toward the elongation zone. CRK5 is a plasma membrane-associated kinase that forms U-shaped patterns facing outer lateral walls of epidermis and cortex cells. Brefeldin inhibition of exocytosis stimulates CRK5 internalization into brefeldin bodies. CRK5 phosphorylates the hydrophilic loop of PIN2 in vitro, and PIN2 shows accelerated accumulation in brefeldin bodies in the crk5 mutant. Delayed gravitropic response of the crk5 mutant thus likely reflects defective phosphorylation of PIN2 and deceleration of its brefeldin-sensitive membrane recycling.

AB - CRK5 is a member of the Arabidopsis thaliana Ca2+/calmodulin-dependent kinase-related kinase family. Here, we show that inactivation of CRK5 inhibits primary root elongation and delays gravitropic bending of shoots and roots. Reduced activity of the auxin-induced DR5-green fluorescent protein reporter suggests that auxin is depleted from crk5 root tips. However, no tip collapse is observed and the transcription of genes for auxin biosynthesis, AUXIN TRANSPORTER/AUXIN TRANSPORTERLIKE PROTEIN (AUX/LAX) auxin influx, and PIN-FORMED (PIN) efflux carriers is unaffected by the crk5 mutation. Whereas AUX1, PIN1, PIN3, PIN4, and PIN7 display normal localization, PIN2 is depleted from apical membranes of epidermal cells and shows basal to apical relocalization in the cortex of the crk5 root transition zone. This, together with an increase in the number of crk5 lateral root primordia, suggests facilitated auxin efflux through the cortex toward the elongation zone. CRK5 is a plasma membrane-associated kinase that forms U-shaped patterns facing outer lateral walls of epidermis and cortex cells. Brefeldin inhibition of exocytosis stimulates CRK5 internalization into brefeldin bodies. CRK5 phosphorylates the hydrophilic loop of PIN2 in vitro, and PIN2 shows accelerated accumulation in brefeldin bodies in the crk5 mutant. Delayed gravitropic response of the crk5 mutant thus likely reflects defective phosphorylation of PIN2 and deceleration of its brefeldin-sensitive membrane recycling.

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