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Updated: Jul 13, 2026

Caspase-3 Activity in the Rat Amygdala Measured by Spectrofluorometry After Myocardial Infarction

Caspase-3 Activity in the Rat Amygdala Measured by Spectrofluorometry After Myocardial Infarction

Published on: January 12, 2016

Matrin 3 is a Ca2+/calmodulin-binding protein cleaved by caspases.

C Alexander Valencia¹, Wujian Ju, Rihe Liu

¹School of Pharmacy and Carolina Center for Genome Sciences, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

Biochemical and Biophysical Research Communications

|July 31, 2007

Summary

Matrin 3, a nuclear protein, binds calmodulin (CaM) in a calcium-dependent manner and is cleaved by caspases. These interactions, occurring near its nuclear localization signal, suggest novel regulatory mechanisms for matrin 3 function.

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Caspase-3 Activity in the Rat Amygdala Measured by Spectrofluorometry After Myocardial Infarction

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Published on: January 12, 2016

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Identifying Caspases and their Motifs that Cleave Proteins During Influenza A Virus Infection

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Published on: July 21, 2022

Area of Science:

Molecular and Cellular Biology
Protein Biochemistry

Background:

Matrin 3 is a nuclear matrix protein involved in RNA anchoring and gene regulation.
Previous studies implicated Matrin 3 in various cellular processes, including PKA signaling.
Its role in response to calcium signaling and proteolytic cleavage remained uncharacterized.

Purpose of the Study:

To characterize the calcium-dependent calmodulin (CaM) binding motif of Matrin 3.
To identify and characterize the caspase cleavage site on Matrin 3.
To elucidate the regulatory potential of CaM binding and caspase cleavage on Matrin 3 function.

Main Methods:

Proteome-wide screening using mRNA-displayed human proteome libraries.
In vitro characterization of protein-protein interactions and enzymatic cleavage sites.
Analysis of Matrin 3 domains, including RNA Recognition Motif (RRM) and Nuclear Localization Signal (NLS).

Main Results:

Matrin 3 was identified as a Ca(2+)-dependent CaM-binding protein.
A specific caspase cleavage site was identified downstream of the NLS.
The CaM-binding motif partially overlaps with the RRM and is located near the NLS.

Conclusions:

Matrin 3 function is potentially regulated by Ca(2+)/CaM interactions.
Caspase-mediated cleavage offers another layer of functional regulation for Matrin 3.
These findings reveal novel mechanisms controlling Matrin 3's role in the nucleus.