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Related Experiment Video

Updated: Feb 22, 2026

Real Time Monitoring of Intracellular Bile Acid Dynamics Using a Genetically Encoded FRET-based Bile Acid Sensor

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Published on: January 4, 2016

Farnesylation-mediated subcellular localization is required for CYP85A2 function.

Muhammad Jamshed¹, Siyu Liang¹, Neil M N Hickerson¹

¹a Department of Biological Sciences , University of Calgary , Calgary , Alberta , Canada.

Plant Signaling & Behavior

|September 27, 2017

Summary

This summary is machine-generated.

Protein farnesylation is crucial for plant development. The C-terminal CaaX motif of CYP85A2 targets it to membranes, ensuring brassinosteroid synthesis and normal plant growth, even without a secretory signal.

Keywords:

Abscisic acid (ABA)brassinosteroids drought tolerance farnesylation secretory signal seed germination sub-cellular localization

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Area of Science:

Plant Molecular Biology
Biochemistry
Plant Physiology

Background:

Protein farnesylation, the addition of a farnesyl group to proteins, plays roles in plant development and stress tolerance.
The precise regulatory mechanisms of farnesylation in these processes remain unclear.
CYP85A2, a cytochrome P450, is essential for brassinolide synthesis and requires farnesylation for function.

Purpose of the Study:

To investigate the roles of the N-terminal secretory signal and C-terminal CaaX motif of CYP85A2 in its function and localization.
To understand how these motifs influence CYP85A2 targeting to endomembrane compartments.
To elucidate the impact of farnesylation motif on brassinosteroid synthesis and plant stress responses.

Main Methods:

Analysis of CYP85A2 targeting to endomembrane compartments.
Assessment of CYP85A2 function in the absence of N-terminal secretory signal or C-terminal CaaX motif.
Phenotypic analysis of plants with modified CYP85A2, including brassinolide levels and response to ABA and drought.

Main Results:

The C-terminal CaaX motif is sufficient for targeting CYP85A2 to membrane compartments, even without an intact N-terminal secretory signal.
Partial rescue of cyp85a2-2 mutant phenotypes was observed when the CaaX motif was present.
Loss of both the CaaX motif and secretory signal resulted in failed membrane targeting and instability of CYP85A2.

Conclusions:

The C-terminal CaaX motif is critical for CYP85A2 localization and stability, mediating its function in brassinosteroid synthesis.
Proper targeting of CYP85A2 to endomembrane compartments is essential for its biological activity and normal plant development.
These findings highlight the importance of protein post-translational modifications like farnesylation in regulating plant hormone pathways and stress responses.