MTLN

Last update 08 May 2025

Basic Info

Synonyms

LEMP, LINC00116, lncRNA-encoded micropeptide

+ [9]

Introduction

Positively regulates mitochondrial complex assembly and/or stability (By similarity). Increases mitochondrial membrane potential while decreasing mitochondrial reactive oxygen species (PubMed:29949756). Increases mitochondrial respiration rate (PubMed:29949756). Increased mitochondrial respiratory activity promotes myogenic differentiation which facilitates muscle growth and regeneration (By similarity). Increases mitochondrial calcium retention capacity (PubMed:29949756). Plays a role in maintenance of cellular lipid composition through its interaction with cytochrome b5 reductase CYB5R3 which is required for mitochondrial respiratory complex I activity (By similarity). Interacts with the mitochondrial trifunctional enzyme complex (MTE) and enhances fatty acid beta-oxidation (PubMed:32243843). Not required for MTE formation or stability (By similarity). Modulates triglyceride clearance in adipocytes through its role in regulating fatty acid beta-oxidation and lipolysis (PubMed:32243843).

100 Clinical Results associated with MTLN

100 Translational Medicine associated with MTLN

0 Patents (Medical) associated with MTLN

Literatures (Medical) associated with MTLN

01 Jan 2025·iScience

Mitoregulin self-associates to form likely homo-oligomeric pore-like complexes

Article

Author: Schnicker, Nicholas J ; Linzer, Connor R ; Xu, Zhen ; Boudreau, Ryan L ; Stein, Colleen S ; Witmer, Nathan H

We and others previously found that a misannotated long noncoding RNA encodes for a conserved mitochondrial transmembrane microprotein named Mitoregulin (Mtln). Beyond an established role for Mtln in lipid metabolism, Mtln has been shown to broadly influence mitochondria, boosting respiratory efficiency and Ca²⁺ retention capacity, while lowering ROS, yet the underlying mechanisms remain unresolved. Prior studies have identified possible Mtln protein interaction partners; however, a lack of consensus persists, and no claims have been made about Mtln's structure. We noted two key published observations that seemingly remained overlooked: 1) endogenous Mtln co-immunoprecipitates with epitope-tagged Mtln at high efficiency, and 2) Mtln primarily appears to exist in a ∼66 kDa complex. To investigate if Mtln may self-oligomerize into higher-order complexes, we performed co-immunoprecipitation, computational modeling, and native gel assessments of Mtln-containing complexes in cells and tissues and tested whether synthetic Mtln protein itself forms oligomeric complexes. Our combined results provide strong support that Mtln self-associates and likely forms a hexameric pore-like structure.

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

Micropeptide MPM regulates cardiomyocyte proliferation and heart growth via the AKT pathway

Article

Author: Chen, Hua-Xing ; Zhuang, Shi-Mei ; Xie, Peng-Peng ; Zhang, Wei ; Lin, Yi-Fang ; Huang, Jie-Yi ; Ma, Yan-Zhen ; Li, Lan-Qi ; Zhu, Ying

The role of micropeptide in cardiomyocyte proliferation remains unknown. We found that MPM (micropeptide in mitochondria) was highly expressed in cardiomyocytes. Compared to MPM^+/+ mice, MPM knockout (MPM^-/-) mice exhibited reduction in left ventricular (LV) mass, myocardial thickness and LV fractional shortening. RNA-sequencing analysis in H9c2, a rat cardiomyocyte cell line, identified downregulation of cell cycle-promoting genes as the most significant alteration in MPM-silencing cells. Consistently, gain- and loss-of-function analyses in H9c2 cells revealed that cardiomyocyte proliferation was repressed by silencing MPM but was promoted by overexpressing MPM. Moreover, the cardiomyocytes in the hearts of MPM^-/- mice displayed reduced proliferation rates. Mechanism investigations disclosed that MPM is crucial for AKT activation in cardiomyocytes. We also identified an interaction between MPM and PTPMT1, and found that silencing PTPMT1 attenuated the effect of MPM in activating the AKT pathway, whereas inhibition of the AKT pathway abrogated the role of MPM in promoting cardiomyocyte proliferation. Collectively, these results indicate that MPM may promote cardiomyocyte proliferation and thus heart growth by interacting with PTPMT1 to activate the AKT pathway. Our findings identify the novel function and regulatory network of MPM and highlight the importance of micropeptides in cardiomyocyte proliferation and heart growth.

01 Nov 2024·Biochemical and Biophysical Research Communications

Mitoregulin modulates inflammation in osteoarthritis: Insights from synovial transcriptomics and cellular studies

Article

Author: Jeon, Jaewan ; Kim, Wanil ; Moon, Sang Won ; Do, Hwan-Kwon ; Min, Ju-Sik ; Choi, Minjeong

Osteoarthritis is a prevalent musculoskeletal disease that involves cartilage degradation, subchondral bone remodeling, and synovial inflammation and ultimately causes physical disability. Common risk factors for osteoarthritis include age, sex, obesity, and genetic predispositions. Treatment includes nonpharmaceutical and pharmacological approaches; however, disease-modifying osteoarthritis drugs remain undeveloped. We aimed to identify key regulatory factors underlying the etiology of osteoarthritis. We studied alterations of the inflammatory responses after manipulating the expression of MTLN, which we selected after sequencing and transcriptomics of the patients' synovial tissues. MTLN expression was increased in synovial tissues of patients and in SW982 human synovial sarcoma cells following inflammatory stimuli. We found that MTLN overexpression or knockout respectively decreased or increased expression of the inflammation-associated genes, including IL-6, IL-8, and TNF-α. Thus, high levels of MTLN in osteoarthritis may protect tissues against excessive inflammation, thereby offering therapeutic potentials.

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MTLN

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