Proteasome-dependent proteolysis has a critical role in fine-tuning the feedback inhibition of cytokinin signaling

Jasmina Kurepa; Yan Li; Jan A. Smalle

doi:10.4161/psb.23474

Proteasome-dependent proteolysis has a critical role in fine-tuning the feedback inhibition of cytokinin signaling

Jasmina Kurepa, Yan Li, Jan A. Smalle

Plant and Soil Sciences

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

The ubiquitin/26S proteasome-dependent proteolysis of response regulators is a critical element of many plant hormone signaling pathways. We have recently shown that cytokinin signaling requires the AXR1 component of the related to ubiquitin (RU B) protein modification pathway to promote the proteasome-dependent degradation of the cytokinin response inhibitor ARR 5. Here, we show that ARR 5 also accumulates in the 26S proteasome mutant rpn12a-1, and leads to a marked resistance to cytokinins. Collectively, these results suggest that proteasome-dependent proteolysis of feedback inhibitors such as ARR 5 is essential for the maintenance of optimal responsivity and plasticity in cytokinin signaling.

Original language	English
Pages (from-to)	e23474.1-e23474.3
Journal	Plant Signaling and Behavior
Volume	8
Issue number	3
DOIs	https://doi.org/10.4161/psb.23474
State	Published - Mar 2013

Bibliographical note

Funding Information:
This work was supported by grants from NIFA/NRI (2005-35304-16043) and NSF (0919991) and the Kentucky Tobacco Research and Development Center.

Keywords

26S proteasome
Cytokinin signaling
Negative feedback regulation
RUB modification pathway
type-A ARRs

ASJC Scopus subject areas

Plant Science

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10.4161/psb.23474

Cite this

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title = "Proteasome-dependent proteolysis has a critical role in fine-tuning the feedback inhibition of cytokinin signaling",

abstract = "The ubiquitin/26S proteasome-dependent proteolysis of response regulators is a critical element of many plant hormone signaling pathways. We have recently shown that cytokinin signaling requires the AXR1 component of the related to ubiquitin (RU B) protein modification pathway to promote the proteasome-dependent degradation of the cytokinin response inhibitor ARR 5. Here, we show that ARR 5 also accumulates in the 26S proteasome mutant rpn12a-1, and leads to a marked resistance to cytokinins. Collectively, these results suggest that proteasome-dependent proteolysis of feedback inhibitors such as ARR 5 is essential for the maintenance of optimal responsivity and plasticity in cytokinin signaling.",

keywords = "26S proteasome, Cytokinin signaling, Negative feedback regulation, RUB modification pathway, type-A ARRs",

author = "Jasmina Kurepa and Yan Li and Smalle, {Jan A.}",

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year = "2013",

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AU - Kurepa, Jasmina

AU - Li, Yan

AU - Smalle, Jan A.

N1 - Funding Information: This work was supported by grants from NIFA/NRI (2005-35304-16043) and NSF (0919991) and the Kentucky Tobacco Research and Development Center.

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AB - The ubiquitin/26S proteasome-dependent proteolysis of response regulators is a critical element of many plant hormone signaling pathways. We have recently shown that cytokinin signaling requires the AXR1 component of the related to ubiquitin (RU B) protein modification pathway to promote the proteasome-dependent degradation of the cytokinin response inhibitor ARR 5. Here, we show that ARR 5 also accumulates in the 26S proteasome mutant rpn12a-1, and leads to a marked resistance to cytokinins. Collectively, these results suggest that proteasome-dependent proteolysis of feedback inhibitors such as ARR 5 is essential for the maintenance of optimal responsivity and plasticity in cytokinin signaling.

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Proteasome-dependent proteolysis has a critical role in fine-tuning the feedback inhibition of cytokinin signaling

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

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