Ask about this productRelated genes to: NHEDC2 antibody
- Gene:
- SLC9B2 NIH gene
- Name:
- solute carrier family 9 member B2
- Previous symbol:
- NHEDC2
- Synonyms:
- FLJ23984, NHA2
- Chromosome:
- 4q24
- Locus Type:
- gene with protein product
- Date approved:
- 2007-05-15
- Date modifiied:
- 2016-02-17
Related products to: NHEDC2 antibody
Related articles to: NHEDC2 antibody
- A key prerequisite of transporter proteins' function is their trafficking to the target cellular membranes where they fulfill distinct physiological roles. Cornichon proteins (CNIH/Erv14) represent a highly conserved family of coat protein complex II (COPII)-coated vesicle cargo receptors that facilitate the exit of numerous transporters from the endoplasmic reticulum (ER) to proceed via the secretory pathway. Despite their biomedical significance, the cargo specificities of the four human cornichons (CNIH1-4) remain largely unexplored. Here, we conducted a bioinformatics analysis of the CNIH/Erv14 family, revealing evolutionary conservation profiles of the family based on an alignment of 1879 sequences. AlphaFold3 modeling predicts that residues identified as the most evolutionarily conserved in cornichon family interact with Sec24 proteins of COPII vesicles. We also demonstrate the suitability of the model yeast Saccharomyces cerevisiae for studying the properties and putative interactors of human cornichons. We engineered S. cerevisiae strains in which the endogenous cornichon gene (ERV14) was replaced with human CNIH1, CNIH2, or CNIH4 coding sequences or CNIH coding sequences were expressed from multi-copy plasmids. The studied human cornichons were functional in S. cerevisiae cells and, to varying extents, complemented the differing phenotypes related to yeast ScErv14 roles in monovalent-cation homeostasis. The presence of human CNIHs supported the functioning of the yeast plasma-membrane Na, K/H antiporter Nha1, a known cargo of ScErv14. Both yeast ScErv14 and human CNIH cornichons improved the plasma-membrane targeting and functioning of the human Na/H antiporter NHA2 in yeast cells, identifying NHA2 as a novel cargo of cornichon COPII cargo receptors. - Source: PubMed
Kacovská KarolínaPapoušková KláraMasrati GalRosas-Santiago PaulPrzeczková TerezaŽárská VeronikaBen-Tal NirZimmermannová Olga - Mitochondrial dysfunction, particularly in energy metabolism, oxidative stress, and apoptosis, has long been implicated in stroke pathogenesis. However, the causal role of specific mitochondrial components remains unclear, especially across distinct stroke subtypes. - Source: PubMed
Publication date: 2025/12/07
Luo JingZheng YalingChen JialeiJiang NingWu JingxianZhang Xiaogang - Epigenetic regulation plays a crucial role in skeletal degenerative diseases, including osteoporosis. As an epigenetic reader, bromodomain protein 4 (Brd4) is known as a key driver of gene activation; however, its role in maintaining skeletal homeostasis remains largely unknown. - Source: PubMed
Wang XiaoheLuo FangjiMiao GuiqiangZheng BoyuanXu ChenhaoWong Vincent Kam WaiPeng YuanshuZeng RongPang JinzhuZhang XuguangJu ZhenyuZha ZhengangWang XiaogangZheng XiaofeiZhang Huan-Tian - Mitochondria are central to immune regulation, inflammation, and cellular metabolism. Growing evidence suggests that mitochondrial dysfunction contributes to autoimmune disease (AD) pathogenesis by modulating inflammatory pathways and immune cell function. However, the causal relationships between mitochondria-related proteins and ADs remain unclear. - Source: PubMed
Publication date: 2025/07/08
Hong Yanggang - The sodium/proton exchanger NHA2, also known as SLC9B2, is important for insulin secretion, renal blood pressure regulation, and electrolyte retention. Recent structures of bison NHA2 has revealed its unique 14-transmembrane helix architecture, which is different from SLC9A/NHE members made up from 13-TM helices. Sodium/proton exchangers are functional homodimers, and the additional N-terminal helix in NHA2 was found to alter homodimer assembly. Here, we present the cryo-electron microscopy structures of apo human NHA2 in complex with a Fab fragment and also with the inhibitor phloretin bound at 2.8 and 2.9 Å resolution, respectively. We show how phosphatidic acid (PA) lipids bind to the homodimer interface of NHA2 on the extracellular side, which we propose has a regulatory role linked to cell volume regulation. The ion binding site of human NHA2 has a salt bridge interaction between the ion binding aspartate D278 and R432, an interaction previously broken in the bison NHA2 structure, and these differences suggest a possible ion coupling mechanism. Lastly, the human NHA2 structure in complex with phloretin offers a template for structure-guided drug design, potentially leading to the development of more selective and potent NHA2 inhibitors. - Source: PubMed
Publication date: 2025/04/29
Jung SukkyeongKokane SurabhiLi HangIwata SoNomura NorimichiDrew David