Ask about this productRelated genes to: LETM1 antibody
- Gene:
- LETM1 NIH gene
- Name:
- leucine zipper and EF-hand containing transmembrane protein 1
- Previous symbol:
- -
- Synonyms:
- SLC55A1
- Chromosome:
- 4p16.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-05-13
- Date modifiied:
- 2017-11-24
Related products to: LETM1 antibody
Related articles to: LETM1 antibody
- Biogenesis and maintenance of the photosynthetic thylakoid membrane requires transport of lipids from their site of synthesis in the chloroplast envelopes to their destination in the thylakoid. While vesicle trafficking is likely involved, we hypothesized a complementary mechanism involving direct membrane interactions. Using domain homology and proteomic profiling of chloroplast membrane fractions, we identified candidate lipid transport proteins present in a distinct, intermediate-density membrane population. This fraction contained an overrepresentation of lipid metabolic enzymes and proteins homologous to known membrane organization factors. Several candidates, including TVP38 FAMILY PROTEIN (TVPFP), PLASMA MEMBRANE FUSION PROTEIN (PMFP), and LETM1-LIKE, localized to discrete subdomains within chloroplasts. Loss-of-function tvpfp or pmfp mutants exhibited altered chloroplast ultrastructure, including changes in thylakoid-envelope proximity, supporting their roles in maintaining membrane architecture. These findings, which identify a chloroplast membrane subdomain enriched in proteins with specialized functions, offer a foundation for elucidating the molecular architecture of these regions. - Source: PubMed
Publication date: 2026/05/19
LaBrant Evan WSmith Cailin NTorres-Gerena Alondra DIshimwe JoslinHuang FanTullis AllanLitterer LaurenModi Bhoomi FNaldrett Michael JAltartouri BaraRoston Rebecca L - Inflammatory bowel disease (IBD) is a chronic, nonspecific inflammatory disorder affecting the gastrointestinal tract. The condition's pathology not only involves the digestive system but also can impact various organs and tissues throughout the body. Metabolic syndrome is a clinical syndrome characterized by obesity, insulin resistance, hypertension, and hyperlipidemia. Extensive research suggests a potential association between IBD and metabolic syndrome. - Source: PubMed
Publication date: 2026/04/14
Yin Yu-ZheYan Chao-ShengWu LingLi Guo-QingPei Xin-YuXue Yu-ZhengRen Yi-LinSun Hao-WenSheng Ying-Yue - Mitochondrial dysfunction is a central contributor to the pathogenesis of intestinal ischemia/reperfusion (I/R) injury. This dysfunction is closely linked to mitochondrial calcium overload and excessive reactive oxygen species (ROS) production, culminating in cellular apoptosis. Leucine Zipper And EF-Hand Containing Transmembrane Protein 1 (LETM1), a key regulator of mitochondrial permeability, is essential for cellular homeostasis and survival. However, the role and underlying mechanism of LETM1 in intestinal I/R injury remain poorly understood. Here, we observed that LETM1 expression was significantly downregulated in intestinal tissues following I/R. AAV9-mediated overexpression of LETM1 significantly alleviated mitochondrial dysfunction. We further found that the acetylation status at lysine 597 (K597) modulates the stability of LETM1 in Caco-2 cells. LETM1 was identified as a downstream target of mitochondrial deacetylase Sirtuin 3 (SIRT3), and its knockdown significantly impaired the protective effects of SIRT3 in vitro. Collectively, our findings provide the first evidence that LETM1 serves as a protective target against calcium overload-induced mitochondrial dysfunction and apoptosis during intestinal I/R injury. These findings highlight the therapeutic potential of targeting LETM1 deacetylation as a novel strategy for intestinal I/R injury prevention. - Source: PubMed
Publication date: 2026/03/10
Wang GuorongZhao XuziFeng YunfeiYang FengyuanLv ChengMi WenjiaZhang XinxinTian XiaofengYao JihongWang Guangzhi - From insects to mammals, essential brain functions, such as forming long-term memories (LTMs), increase metabolic activity in stimulated neurons to meet the energetic demand associated with brain activation. However, while impairing neuronal metabolism limits brain performance, whether expanding the metabolic capacity of neurons boosts brain function remains poorly understood. Here, we show that LTM formation of flies and mice can be enhanced by increasing mitochondrial metabolism in central memory circuits. By knocking down the mitochondrial Ca exporter Letm1, we favour Ca retention in the mitochondrial matrix of neurons due to reduction of mitochondrial H/Ca exchange. The resulting increase in mitochondrial Ca over-activates mitochondrial metabolism in neurons of central memory circuits, leading to improved LTM storage in training paradigms in which wild-type counterparts of both species fail to remember. Our findings unveil an evolutionarily conserved mechanism that controls mitochondrial metabolism in neurons and indicate its involvement in shaping higher brain functions, such as LTM. - Source: PubMed
Publication date: 2026/02/11
Amrapali Vishwanath AnjaliComyn TyphaineMira Rodrigo GBrossier ClairePascual-Caro CarlosFaour MayaBoumendil KahinaChintaluri ChaitanyaRamon-Duaso CarlaFan RuolinGhosh KishalayFarrants HelenBerwick Jean-PaulSivakumar RiyaLopez-Manzaneda MarioSchreiter Eric RPreat ThomasVogels Tim PRangaraju VidhyaBusquets-Garcia ArnauPlaçais Pierre-YvesPavlowsky Alicede Juan-Sanz Jaime - Mitochondria are dynamic organelles that undergo repeated fusion and fission. We studied how the distribution and shape of mitochondria change during spermatogenesis and whether factors that regulate their dynamics are necessary for these changes. Unlike the shortened mitochondria seen in mitosis, an interconnected network of elongated mitochondria forms before meiosis and is maintained during meiotic divisions. Mitochondria are evenly divided into daughter cells, relying on microtubules and F-actin. To explore the role of mitochondrial network structure in cell growth and meiosis, we depleted the mitochondrial fusion factors Opa1 and Marf and the morphology proteins Letm1 and EndoB in spermatocytes. This knockdown led to inhibited cell growth and failed meiosis. As a result, the spermatocytes differentiated into spermatids without completing meiosis. The knockdown also inhibited the cytoplasmic and nuclear accumulation of Cyclin B before meiosis, and Cdk1 was not fully activated at the onset of meiosis. Notably, ectopic overexpression of Cyclin B partially rescued the failure of meiosis. Many spermatids from the spermatocytes subjected to the knockdowns contained multiple smaller nuclei and abnormally shaped Nebenkerns. These findings suggest that mitochondrial network structure, maintained by fusion and morphology factors, is essential for meiosis progression and Nebenkern formation in spermatogenesis. - Source: PubMed
Publication date: 2025/10/14
Matsuo TatsuruYamanaka MitsukiInoue Yoshihiro H