Ask about this productRelated genes to: TOM1 antibody
- Gene:
- TOM1 NIH gene
- Name:
- target of myb1 membrane trafficking protein
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 22q12.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-14
- Date modifiied:
- 2016-10-05
Related products to: TOM1 antibody
Related articles to: TOM1 antibody
- There is a need for objective biomarkers of dietary potassium. The mechanisms through which dietary potassium influences kidney health are incompletely understood. - Source: PubMed
Publication date: 2025/09/18
Yang JiaqiBernard LaurenChen JingshaSullivan Valerie KYu BingRhee Eugene PWelling Paul ARebholz Casey M - A recently described G307D variant of the endosomal adaptor protein TOM1 causes severe early-onset multiorgan autoimmunity and combined immunodeficiency. By combining biophysical, biochemical and cell culture experiments, we show that the variant causes a defect in the interaction between TOM1 and TOLLIP, another adaptor protein involved in cargo trafficking and regulation of innate immunity. The G307D variant impairs the ability of TOM1 to reduce TOLLIP phosphatidylinositol 3-phosphate binding, an important regulatory mechanism for cargo trafficking commitment for both proteins. Our experiments using TOM1 G307D patient cells suggested that the variant affects autophagy, seen as an aggravated response to amino acid starvation and accumulation of autophagosomes due to autophagosome-lysosome fusion defect. In addition, inflammatory pathways showed excessive activation in TOM1 G307D patient cells. Our data suggest that the interaction between TOM1 and TOLLIP has a role in the regulation of the human immune system and highlight the importance of fundamental cellular functions, such as cargo trafficking, in controlling immune responses. Our study also provides insights into the caveats of immunomodulatory and stem cell therapies in patients with TOM1 pathogenic variants. - Source: PubMed
Publication date: 2025/09/30
Lång Heljä K MRoach Tiffany GHölttä MaaritKeskitalo SallaVarjosalo MarkkuHeiskanen KaarinaCollins Megan VSeppänen Mikko R JCapelluto Daniel G SIkonen ElinaRyhänen Samppa J - This study aims to explore the therapeutic effects of Astragali Radix-Descurainiae Semen (AR-DS) on heart failure and elucidate the mechanisms behind its efficacy. - Source: PubMed
Publication date: 2025/07/04
Wang MengyueNi SonglinWang TongSun MoWu QiaolanWu XiaolinLu GuangyingSu PeiweiGao ZuChen Qian - Chemoradiation prior to surgery in locally advanced rectal cancer is the current standard therapy but is not effective in all rectal cancer patients. Prognostic markers supporting patient stratification with respect to clinical response would therefore be desirable. The aim of this study was to investigate pathophysiological mechanisms underlying radioresistance and to identify potential prognostic markers by comparative proteome profiling. Therefore, formalin fixed paraffin-embedded tissue (FFPE) samples from rectal tumors ( = 50) and normal control tissue ( = 39) of nonresponders and responders to neoadjuvant chemoradiation were analyzed. As a result, 1685 robustly identified proteins were further evaluated. Comparing tumor with corresponding control samples revealed 221 differentially expressed proteins (FDR < 0.05) with FTL, PCOLCE, and RCN3 being most striking in tumor tissue. CEACAM 1, 5, and 6, as well as MCM protein complex components, were significantly up-regulated in tumor tissue of nonresponders. The autophagic activity-related and DNA damage repair proteins TOM1, CAPNS1, TP53BP1, HS1BP3, as well as COTL1 and DCPS, discriminated non- and nearly complete from complete responders. In the tumor-surrounding tissue of nonresponders, the innate immune response-suppressing protein CD55 was found specifically up-regulated. These proteins may serve as prognostic markers and potential therapeutic targets, requiring further validation in prospective studies. - Source: PubMed
Publication date: 2025/06/26
Zott TobiasWolf MichaelPlessl-Walder GünterRegele HeinzBergmann MichaelMeier-Menches Samuel MGerner ChristopherSilberhumer Gerd RBileck Andrea - Homologous to E6AP C terminus (HECT) ubiquitin ligases play key roles in essential pathways such as DNA repair, cell cycle control, or protein quality control. Tom1 is one of five HECT ubiquitin E3 ligases in budding yeast S. cerevisiae and is prototypical for a ligase with pleiotropic functions such as ubiquitin chain amplification, orphan quality control, and DNA damage response. Structures of full-length HECT ligases, including the Tom1 ortholog HUWE1, have been reported, but how domains beyond the conserved catalytic module contribute to catalysis remains largely elusive. Here, through cryoelectron microscopy (cryo-EM) snapshots of Tom1 during an active ubiquitination cycle, we demonstrate that the extended domain architecture directly contributes to activity. We identify a Tom1-ubiquitin architecture during ubiquitination involving a non-canonical ubiquitin-binding site in the solenoid shape of Tom1. We demonstrate that this ubiquitin-binding site coordinates a structural ubiquitin contributing to the fidelity of K48 poly-ubiquitin chain assembly. - Source: PubMed
Publication date: 2025/05/12
Warner KatrinaHunkeler MoritzBaek KheewoongSchmoker AnnaRoy Burman Shourya SOverwijn DaanJin CyrusDonovan Katherine AFischer Eric S