TMEM223

Last update 08 May 2025

Basic Info

Synonyms

MGC3196, TMEM223, transmembrane protein 223

Introduction

Mitochondrial ribosome-associated protein involved in the first steps of cytochrome c oxidase complex (complex IV) biogenesis (PubMed:34969438). Stimulates the translation of MT-CO1 mRNA and is a constituent of early MT-CO1 assembly intermediates (PubMed:34969438).

100 Clinical Results associated with TMEM223

100 Translational Medicine associated with TMEM223

0 Patents (Medical) associated with TMEM223

Literatures (Medical) associated with TMEM223

01 Aug 2020·Biochimica et Biophysica Acta (BBA) - BioenergeticsQ2 · BIOLOGY

TMEM70 functions in the assembly of complexes I and V

Q2 · BIOLOGY

Article

Author: Leo G.J. Nijtmans ; Mariel van den Brand ; Martijn A. Huynen ; Laura Sánchez-Caballero ; Teunis J.P. van Dam ; Sergio Guerrero-Castillo ; Richard Rodenburg ; Joeri van Strien ; Ulrich Brandt ; Dei M. Elurbe ; Fabian Baertling

Protein complexes from the oxidative phosphorylation (OXPHOS) system are assembled with the help of proteins called assembly factors. We here delineate the function of the inner mitochondrial membrane protein TMEM70, in which mutations have been linked to OXPHOS deficiencies, using a combination of BioID, complexome profiling and coevolution analyses. TMEM70 interacts with complex I and V and for both complexes the loss of TMEM70 results in the accumulation of an assembly intermediate followed by a reduction of the next assembly intermediate in the pathway. This indicates that TMEM70 has a role in the stability of membrane-bound subassemblies or in the membrane recruitment of subunits into the forming complex. Independent evidence for a role of TMEM70 in OXPHOS assembly comes from evolutionary analyses. The TMEM70/TMEM186/TMEM223 protein family, of which we show that TMEM186 and TMEM223 are mitochondrial in human as well, only occurs in species with OXPHOS complexes. Our results validate the use of combining complexome profiling with BioID and evolutionary analyses in elucidating congenital defects in protein complex assembly.

01 Jan 2020·Technology in Cancer Research & TreatmentQ4 · MEDICINE

Paclitaxel Promotes Tumor-Infiltrating Macrophages in Breast Cancer

Q4 · MEDICINE

ArticleOA

Author: Hu, Shufang ; Li, Zhaoqing ; Shen, Jun ; Chen, Cong

Objective: Breast cancer remains the most threatening triggers of cancer death in women. Drug resistance inevitably leads to the weakness of treatment for breast cancer. Macrophages, as one of the most abundant immune cells in tumor immune-infiltrating microenvironment, involves in cell survival, migration, and invasion of breast cancer. Methods: In this study, we compared the proportions of macrophages in patients with breast cancer with and without paclitaxel treatment, and investigated the targeted genes associated with macrophages for paclitaxel response. To explore the relationship between drug-related genes and breast cancer prognosis, survival analysis based on the drug-related genes were performed by website of Kaplan-Meier plotter with the threshold of significant P value < .05. Results: Compared to the normal samples, we revealed that paclitaxel significantly enhanced the ratio of macrophages in the tumor microenvironment. Furthermore, the expression of 3 drug-related genes (IFT46, PEX11A, and TMEM223) were significantly negatively associated with the proportions of macrophages. And it is worth to notice that PEX11A and TMEM223 were associated with better progression-free survival outcomes of patients with breast cancer. Moreover, PEX11A was associated with longer overall survival time of breast cancer. Conclusion: Taken all together, all the findings support to gain a better understanding to the development of more effective therapies targeted with paclitaxel.

01 Jun 2019·Pflügers Archiv - European Journal of PhysiologyQ4 · MEDICINE

Four novel interaction partners demonstrate diverse modulatory effects on voltage-gated CaV2.2 Ca2+ channels

Q4 · MEDICINE

Article

Author: Pavlovicova, Michaela ; Jurkovicova-Tarabova, Bohumila ; Klugbauer, Norbert ; Moravcik, Roman ; Ondacova, Katarina ; Kominkova, Viera ; Moravcikova, Lucia ; Lichvarova, Lucia ; Lacinova, Lubica ; Mallmann, Robert

Voltage-gated Ca²⁺ channels are embedded in a network of protein interactions that are fundamental for channel function and modulation. Different strategies such as high-resolution quantitative MS analyses and yeast-two hybrid screens have been used to uncover these Ca²⁺ channel nanodomains. We applied the yeast split-ubiquitin system with its specific advantages to search for interaction partners of the Ca_V2.2 Ca²⁺ channel and identified four proteins: reticulon 1 (RTN1), member 1 of solute carrier family 38 (SLC38), prostaglandin D2 synthase (PTGDS) and transmembrane protein 223 (TMEM223). Interactions were verified using the yeast split-ubiquitin system and narrowed down to Ca_V2.2 domain IV. Colocalization studies using fluorescent constructs demonstrated defined regions of subcellular localization. Detailed electrophysiological studies revealed that coexpression of RTN1 modulated Ca_V2.2 channels only to a minor extent. SLC38 accelerated the cumulative current inactivation during a high-frequency train of brief depolarizing pulses. As neurons expressing Ca_V2.2 channels were exposed to high-frequency bursts under physiological conditions, observed regulation may have a negative modulatory effect on transmitter release. Coexpression of PTGDS significantly lowered the average current density and slowed the kinetics of cumulative current inactivation. Since the latter effect was not significant, it may only partly compensate the first one under physiological conditions. Expression of TMEM223 lowered the average current density, accelerated the kinetics of cumulative current inactivation and slowed the kinetics of recovery from inactivation. Therefore, TMEM223 and, to a lesser extent, PTGDS, may negatively modulate Ca²⁺ entry required for transmitter release and/or for dendritic plasticity under physiological conditions.

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