Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Cell Signaling in Plants

Cell Signaling in Plants

Plant cells communicate to coordinate their cycle of growth, flowering and fruiting, and activities in roots, shoots, and leaves in response to the changing environmental conditions. Plant signaling is distinct from animal signaling. Plants primarily utilize enzyme-linked receptors, whereas the largest class of cell-surface receptors in animals are G-protein coupled receptors (GPCRs). Unlike animals, receptor tyrosine kinases are rare in plants. Instead, plants have a diverse class of...

Regulated Protein Degradation

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...

Regulated Protein Degradation

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...

Amplifying Signals via Enzymatic Cascade

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...

Regulation of the Unfolded Protein Response

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...

Interactions Between Signaling Pathways

Interactions Between Signaling Pathways

Signaling cascades usually lack linearity. Multiple pathways interact and regulate one another, allowing cells to integrate and respond to diverse environmental stimuli.
Convergence and divergence, and cross-talk between signaling pathways
Two distinct signaling pathways can converge on a single functional unit, which may either be a single protein or a complex of proteins. The response is either functionally distinct or synergistic between the two pathways but different from the response...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Development of In Vitro and In Planta Strategies for Efficient Production of High-Value Steviol Glycosides.

Plant biotechnology journal·2026

Same author

Beyond the CO-FT regulatory module: E1 and PHYA emerge as players in photoperiodic regulation of flowering in legumes.

Journal of experimental botany·2026

Same author

Shoot transcriptome and co-expression network analysis of African rice cultivars identify drought-tolerance hub genes and growth stage-dependent trade-offs.

Frontiers in plant science·2026

Same author

In Vivo Detection of IAA Using IAA Nanosensor.

Methods in molecular biology (Clifton, N.J.)·2026

Same author

Analysis of Nanosensor-Reported Waveforms for Plant Wounding.

Nano letters·2026

Same author

HFR1 delays dark-induced leaf senescence by suppressing ORE1 transcription and attenuating its protein activity.

Plant physiology·2026

Search research articles

Related Experiment Video

Updated: Jun 27, 2026

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

Regulated proteolysis in light-related signaling pathways.

Rossana Henriques¹, In-Cheol Jang, Nam-Hai Chua

¹Laboratory of Plant Molecular Biology, The Rockefeller University, New York, NY 10065, USA.

Current Opinion in Plant Biology

|December 17, 2008

Summary

Ubiquitination, a protein modification, regulates plant light signaling. This process controls key developmental pathways like photomorphogenesis and flowering time.

More Related Videos

Assaying Proteasomal Degradation in a Cell-free System in Plants

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Related Experiment Videos

Last Updated: Jun 27, 2026

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Light-mediated Reversible Modulation of the Mitogen-activated Protein Kinase Pathway during Cell Differentiation and Xenopus Embryonic Development

Published on: June 15, 2017

Assaying Proteasomal Degradation in a Cell-free System in Plants

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Area of Science:

Plant Biology
Molecular Biology
Biochemistry

Background:

Post-translational modifications regulate protein function and levels.
Ubiquitination, the attachment of ubiquitin, typically targets proteins for degradation.
Plant signaling pathways are complex and involve intricate regulatory mechanisms.

Purpose of the Study:

To review recent advances in understanding ubiquitination's role in plant light signaling.
To highlight the impact of ubiquitin-mediated proteolysis on photomorphogenesis, circadian clock, and flowering time.

Main Methods:

Literature review of recent studies on plant ubiquitination.
Focus on ubiquitin-mediated proteolysis in light signaling pathways.

Main Results:

Ubiquitination is a key regulator of protein turnover in plant light responses.
Specific examples illustrate its role in photomorphogenesis, circadian rhythms, and flowering.
Ubiquitin-mediated proteolysis fine-tunes light-dependent developmental processes.

Conclusions:

Ubiquitination is crucial for precise control of plant light signaling pathways.
Targeted protein degradation via ubiquitination is essential for plant development and adaptation to light conditions.