MRLN

Last update 08 May 2025

Basic Info

Synonyms

Linc-RAM, LINC00948, M1

+ [4]

Introduction

Inhibits the activity of ATP2A1/SERCA1 ATPase in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+), thereby acting as a key regulator of skeletal muscle activity. Its high expression in adult skeletal muscle, suggests that it constitutes the predominant regulator of ATP2A1/SERCA1 in adult skeletal muscle. Also inhibits the activity of ATP2A2/SERCA2 and ATP2A3/SERCA3.

100 Clinical Results associated with MRLN

100 Translational Medicine associated with MRLN

0 Patents (Medical) associated with MRLN

Literatures (Medical) associated with MRLN

01 Apr 2024·Peptides

Cardiac effects of myoregulin in ischemia-reperfusion

Article

Author: Byers, Mathew S ; Richards, A Mark ; Aitken-Buck, Hamish M ; Holdaway, Mark S ; Pemberton, Christopher J ; Frampton, Chris M ; Paton, Louise N ; Appleby, Sarah ; Lamberts, Regis R

Myoregulin is a recently discovered micropeptide that controls calcium levels by inhibiting the intracellular calcium pump sarco-endoplasmic reticulum Ca²⁺-ATPase (SERCA). Keeping calcium levels balanced in the heart is essential for normal heart functioning, thus myoregulin has the potential to be a crucial regulator of cardiac muscle performance by reducing the rate of intracellular Ca²⁺ uptake. We provide the first report of myoregulin mRNA expression in human heart tissue, absence of expression in human plasma, and the effects of myoregulin on cardiac hemodynamics in an ex vivo Langendorff isolated rat heart model of ischemia/reperfusion. In this preliminary study, myoregulin provided a cardio-protective effect, as assessed by preservation of left ventricular contractility and relaxation, during ischemia/reperfusion. This study provides the foundation for future research in this area.

01 Jan 2024·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Replacement of Lys27 by asparagine in the SERCA regulator myoregulin: A Ca2+ affinity modulator or a catalytic activity switch?

Review

Author: Guerrero-Serna, Guadalupe ; Rathod, Nishadh ; Espinoza-Fonseca, L Michel ; Young, Howard S

Myoregulin (MLN) is a protein that regulates the activity of the sarcoplasmic reticulum Ca²⁺-ATPase (SERCA) without affecting its affinity for Ca²⁺. MLN's residue Lys27 is located at a site where other SERCA regulators control Ca²⁺ affinity. Therefore, we conducted atomistic simulations and ATPase activity experiments to determine whether replacing Lys27 with asparagine, a conserved residue found in various muscle SERCA regulators, would enable MLN to modulate both the Ca²⁺ affinity and catalytic activity of SERCA. Our findings indicate that replacing Lys27 with Asn significantly enhances the inhibitory potency of MLN, but it does not affect SERCA's affinity for Ca²⁺. We suggest that the SERCA site modulating Ca²⁺ affinity also acts as a catalytic activity switch. Therefore, this site is a key element contributing to the functional divergence among homologous SERCA regulators. This study paves the way for future investigations to explore how biological function diverges during the evolution of the SERCA regulator family.

18 Apr 2023·Biochemistry

Functional Role of an Unusual Transmembrane Acidic Residue in the Calcium Pump Regulator Myoregulin.

Article

Author: Young, Howard S ; Guerrero-Serna, Guadalupe ; Liu, Andy Y ; Espinoza-Fonseca, L Michel ; Rathod, Nishadh

Myoregulin (MLN) is a member of the regulin family, a group of homologous membrane proteins that bind to and regulate the activity of the sarcoplasmic reticulum Ca²⁺-ATPase (SERCA). MLN, which is expressed in skeletal muscle, contains an acidic residue in its transmembrane domain. The location of this residue, Asp35, is unusual because the relative occurrence of aspartate is very rare (<0.2%) within the transmembrane helix regions. Therefore, we used atomistic simulations and ATPase activity assays of protein co-reconstitutions to probe the functional role of MLN residue Asp35. These structural and functional studies showed Asp35 has no effects on SERCA's affinity for Ca²⁺ or the structural integrity of MLN in the lipid bilayer. Instead, Asp35 controls SERCA inhibition by populating a bound-like orientation of MLN. We propose Asp35 provides a functional advantage over other members of the regulin family by populating preexisting MLN conformations required for MLN-specific regulation of SERCA. Overall, this study provides new clues about the evolution and functional divergence of the regulin family and offers novel insights into the functional role of acidic residues in transmembrane protein domains.

Analysis

Perform a panoramic analysis of this field.

view full example data

AI Agents Built for Biopharma Breakthroughs

Accelerate discovery. Empower decisions. Transform outcomes.

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

MRLN

Basic Info

Related

Analysis