Dimerization and endocytosis of the sucrose transporter StSUT1 in mature sieve elements

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Dimerization and endocytosis of the sucrose transporter StSUT1 in mature sieve elements. / Liesche, Johannes; Schulz, Alexander; Krügel, Undine; Grimm, Bernhard; Kühn, Christina.

In: Plant Signalling & Behavior, Vol. 3, No. 12, 2008, p. 1136-1137.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Liesche, J, Schulz, A, Krügel, U, Grimm, B & Kühn, C 2008, 'Dimerization and endocytosis of the sucrose transporter StSUT1 in mature sieve elements', Plant Signalling & Behavior, vol. 3, no. 12, pp. 1136-1137. https://doi.org/10.4161/psb.3.12.7096

APA

Liesche, J., Schulz, A., Krügel, U., Grimm, B., & Kühn, C. (2008). Dimerization and endocytosis of the sucrose transporter StSUT1 in mature sieve elements. Plant Signalling & Behavior, 3(12), 1136-1137. https://doi.org/10.4161/psb.3.12.7096

Vancouver

Liesche J, Schulz A, Krügel U, Grimm B, Kühn C. Dimerization and endocytosis of the sucrose transporter StSUT1 in mature sieve elements. Plant Signalling & Behavior. 2008;3(12):1136-1137. https://doi.org/10.4161/psb.3.12.7096

Author

Liesche, Johannes ; Schulz, Alexander ; Krügel, Undine ; Grimm, Bernhard ; Kühn, Christina. / Dimerization and endocytosis of the sucrose transporter StSUT1 in mature sieve elements. In: Plant Signalling & Behavior. 2008 ; Vol. 3, No. 12. pp. 1136-1137.

Bibtex

@article{7758cfa540284c22aa827b6d9f2c4c55,
title = "Dimerization and endocytosis of the sucrose transporter StSUT1 in mature sieve elements",
abstract = "The sucrose transporter StSUT1 from Solanum tuberosum was shown to be regulated post-translationally by redox reagents. Its activity is increased at least 10-fold in the presence of oxidizing agents if expressed in yeast. Oxidation has also an effect on plasma membrane targeting and dimerization of the protein. In response to oxidizing agents, StSUT1 is targeted to lipid raft-like microdomains and SUT1 protein is detectable in the detergent resistant membrane fraction of plant plasma membranes. Interestingly, StSUT1 treated with brefeldin A seems to aggregate in endocytic compartments in mature sieve elements.1 Further analysis of SUT1 targeting will certainly provide more information about the putative involvement of lipid raft-like microdomains in endocytic events. We provide here additional information on the dimerization and endocytosis of the SUT1 protein. The oligomerization of overexpressed SoSUT1 from Spinacia oleracea in transgenic potato plants was analyzed by two-dimensional gel electrophoresis and endocytosis of the StSUT1 protein was confirmed by immunogold labeling.",
author = "Johannes Liesche and Alexander Schulz and Undine Kr{\"u}gel and Bernhard Grimm and Christina K{\"u}hn",
year = "2008",
doi = "10.4161/psb.3.12.7096",
language = "English",
volume = "3",
pages = "1136--1137",
journal = "Plant Signalling & Behavior",
issn = "1559-2316",
publisher = "Taylor & Francis",
number = "12",

}

RIS

TY - JOUR

T1 - Dimerization and endocytosis of the sucrose transporter StSUT1 in mature sieve elements

AU - Liesche, Johannes

AU - Schulz, Alexander

AU - Krügel, Undine

AU - Grimm, Bernhard

AU - Kühn, Christina

PY - 2008

Y1 - 2008

N2 - The sucrose transporter StSUT1 from Solanum tuberosum was shown to be regulated post-translationally by redox reagents. Its activity is increased at least 10-fold in the presence of oxidizing agents if expressed in yeast. Oxidation has also an effect on plasma membrane targeting and dimerization of the protein. In response to oxidizing agents, StSUT1 is targeted to lipid raft-like microdomains and SUT1 protein is detectable in the detergent resistant membrane fraction of plant plasma membranes. Interestingly, StSUT1 treated with brefeldin A seems to aggregate in endocytic compartments in mature sieve elements.1 Further analysis of SUT1 targeting will certainly provide more information about the putative involvement of lipid raft-like microdomains in endocytic events. We provide here additional information on the dimerization and endocytosis of the SUT1 protein. The oligomerization of overexpressed SoSUT1 from Spinacia oleracea in transgenic potato plants was analyzed by two-dimensional gel electrophoresis and endocytosis of the StSUT1 protein was confirmed by immunogold labeling.

AB - The sucrose transporter StSUT1 from Solanum tuberosum was shown to be regulated post-translationally by redox reagents. Its activity is increased at least 10-fold in the presence of oxidizing agents if expressed in yeast. Oxidation has also an effect on plasma membrane targeting and dimerization of the protein. In response to oxidizing agents, StSUT1 is targeted to lipid raft-like microdomains and SUT1 protein is detectable in the detergent resistant membrane fraction of plant plasma membranes. Interestingly, StSUT1 treated with brefeldin A seems to aggregate in endocytic compartments in mature sieve elements.1 Further analysis of SUT1 targeting will certainly provide more information about the putative involvement of lipid raft-like microdomains in endocytic events. We provide here additional information on the dimerization and endocytosis of the SUT1 protein. The oligomerization of overexpressed SoSUT1 from Spinacia oleracea in transgenic potato plants was analyzed by two-dimensional gel electrophoresis and endocytosis of the StSUT1 protein was confirmed by immunogold labeling.

U2 - 10.4161/psb.3.12.7096

DO - 10.4161/psb.3.12.7096

M3 - Journal article

C2 - 19704459

VL - 3

SP - 1136

EP - 1137

JO - Plant Signalling & Behavior

JF - Plant Signalling & Behavior

SN - 1559-2316

IS - 12

ER -

ID: 86211714