The cyclic nucleotide gated cation channel AtCNGC10 traffics from the ER via Golgi vesicles to the plasma membrane of Arabidopsis root and leaf cells

Christopher, David A.; Borsics, Tamás; Yuen, Christen Y. L.; Ullmer, Wendy Elizabeth; Andeme-Ondzighi, Christine; Andrés, Míriam; Kang, Byung-Ho; Staehelin, L. Andrew

doi:10.1186/1471-2229-7-48

Cited by 63 publications

(38 citation statements)

References 32 publications

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“…The resulting fusion protein was shown by fluorescence microscopy (Fig. 1A) to adopt a pattern very similar to previously published examples of proteins that reached the plasma membrane of HEK cells (Christopher et al, 2007;Tang et al, 2007;Mikosch et al, 2009). The expression pattern of free GFP is shown for comparison (Fig.…”

Section: Subcellular Localization Of Glr34 Expressed In Mammalian Ansupporting

confidence: 81%

Ca2+ Conduction by an Amino Acid-Gated Ion Channel Related to Glutamate Receptors

2012

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Section: Subcellular Localization Of Glr34 Expressed In Mammalian Ansupporting

confidence: 81%

Ca2+ Conduction by an Amino Acid-Gated Ion Channel Related to Glutamate Receptors

2012

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“…For neither AtCNGC11 nor 12 could any expression be detected in the root (Fig. 2B, 6–9, 16–19. (Note: the dark areas in the root tips are not GUS staining.…”

Section: Resultsmentioning

confidence: 99%

The cyclic nucleotide-gated channels AtCNGC11 and 12 are involved in multiple Ca2+-dependent physiological responses and act in a synergistic manner

Urquhart

Chin

Ung

et al. 2011

Journal of Experimental Botany

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Arabidopsis cyclic nucleotide-gated ion channels (AtCNGCs) form a large family consisting of 20 members. These channels have so far been reported to be involved in a diverse range of physiological phenomena. For example, AtCNGC18 was reported to play an important role in pollen tube growth, while AtCNGC2, 4, 11, and 12 were implicated in mediating pathogen defence. To identify additional functions for AtCNGC11 and 12, various physiological aspects were analysed using both AtCNGC11 and 12 single knockout mutants as well as a double mutant. Although AtCNGC11 and 12 can function as K+ and Ca2+ channels in yeast, it was found that the loss of AtCNGC11 and 12 in Arabidopsis caused increased sensitivity to Ca2+ but not K+, indicating a specific function for these genes in Ca2+ signalling in planta. However, they did not show an alteration in Ca2+ accumulation, suggesting that AtCNGC11 and 12 are not involved in general Ca2+ homeostasis but rather in the endogenous movement of Ca2+ and/or Ca2+ signalling. Furthermore, these channels synergistically contribute to the generation of a Ca2+ signal that leads to gravitropic bending. Finally, AtCNGC11 and 12 gene expression was induced during dark-induced senescence and AtCNGC11 and 12 knockout mutants displayed enhanced chlorophyll loss, which was even more pronounced in the double mutant, also indicating synergistic roles in senescence. The findings indicate that (i) some CNGC family members have multiple physiological functions and (ii) some plant CNGCs share the same biological function and work in a synergistic manner.

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“…Construct 35S: PDI2-GFP(S65T) was created by inserting the genomic DNA sequence of PDI2 between the NcoI and NdeI sites, and the GFP(S65T) coding sequence between the NdeI and BstEII sites, of plasmid 35S:CNGC10-EGFP (Christopher et al, 2007). The PDI2 fragment was amplified from wildtype Col-0 genomic DNA with primers D and E. The GFP(S65T) fragment was amplified from plasmid HBT95::sGFP(S65T)-NOS with primers L and M. Construct 35S:PDI2-GFP(S65T)+KDEL was generated by replacing the GFP(S65T) fragment of 35S:PDI2-GFP(S65T) with a modified version of GFP(S65T), amplified using primers L and N, which alters the C-terminus of the encoded product from MDELYK to KDEL.…”

Section: Co-immunoprecipitation Of Two-hybrid Positive Isolates With mentioning

confidence: 99%

Protein Disulfide Isomerase-2 of Arabidopsis Mediates Protein Folding and Localizes to Both the Secretory Pathway and Nucleus, Where It Interacts with Maternal Effect Embryo Arrest Factor

Cho

Yuen

Kang

et al. 2011

Molecules and Cells

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Protein disulfide isomerase (PDI) is a thiodisulfide oxidoreductase that catalyzes the formation, reduction and rearrangement of disulfide bonds in proteins of eukaryotes. The classical PDI has a signal peptide, two CXXCcontaining thioredoxin catalytic sites (a,a′), two noncatalytic thioredoxin fold domains (b,b′), an acidic domain (c) and a C-terminal endoplasmic reticulum (ER) retention signal. Although PDI resides in the ER where it mediates the folding of nascent polypeptides of the secretory pathway, we recently showed that PDI5 of Arabidopsis thaliana chaperones and inhibits cysteine proteases during trafficking to vacuoles prior to programmed cell death of the endothelium in developing seeds. Here we describe Arabidopsis PDI2, which shares a primary structure similar to that of classical PDI. Recombinant PDI2 is imported into ER-derived microsomes and complements the E. coli protein-folding mutant, dsbA. PDI2 interacted with proteins in both the ER and nucleus, including ER-resident protein folding chaperone, BiP1, and nuclear embryo transcription factor, MEE8. The PDI2-MEE8 interaction was confirmed to occur in vitro and in vivo. Transient expression of PDI2-GFP fusions in mesophyll protoplasts resulted in labeling of the ER, nucleus and vacuole. PDI2 is expressed in multiple tissues, with relatively high expression in seeds and root tips. Immunoelectron microscopy with GFP-and PDI2-specific antisera on transgenic seeds (PDI2-GFP) and wild type roots demonstrated that PDI2 was found in the secretory pathway (ER, Golgi, vacuole, cell wall) and the nuclei. Our results indicate that PDI2 mediates protein folding in the ER and has new functional roles in the nucleus.

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The cyclic nucleotide gated cation channel AtCNGC10 traffics from the ER via Golgi vesicles to the plasma membrane of Arabidopsis root and leaf cells

Cited by 63 publications

References 32 publications

Ca2+ Conduction by an Amino Acid-Gated Ion Channel Related to Glutamate Receptors

Ca2+ Conduction by an Amino Acid-Gated Ion Channel Related to Glutamate Receptors

The cyclic nucleotide-gated channels AtCNGC11 and 12 are involved in multiple Ca2+-dependent physiological responses and act in a synergistic manner

Protein Disulfide Isomerase-2 of Arabidopsis Mediates Protein Folding and Localizes to Both the Secretory Pathway and Nucleus, Where It Interacts with Maternal Effect Embryo Arrest Factor

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