Ask about this productRelated genes to: FAM84B antibody
- Gene:
- LRATD2 NIH gene
- Name:
- LRAT domain containing 2
- Previous symbol:
- FAM84B
- Synonyms:
- BCMP101, NSE2
- Chromosome:
- 8q24.21
- Locus Type:
- gene with protein product
- Date approved:
- 2005-07-28
- Date modifiied:
- 2019-03-01
Related products to: FAM84B antibody
Related articles to: FAM84B antibody
- Breast cancer (BC) occurs predominantly in women and leads to numerous deaths every year. The identification of effective therapeutic targets will benefit BC patients and increase the likelihood of finding a cure. Family with similar sequence 84, member B (FAM84B) has been implicated in the progression of many kinds of cancers, but its function in BC remains to be explored. In this study, online database analysis revealed that FAM84B expression was higher in BC patient tissues, especially in luminal BC tissues, than in the corresponding normal tissues; furthermore, increased FAM84B expression was related to poor prognosis. Additionally, western blot (WB) analysis revealed that the FAM84B protein was highly expressed in luminal BC cell lines compared to normal and basal-like BC cell lines. Moreover, clinical BC patient tissues were collected and subjected to WB and immunohistochemical (IHC) analyses, and the results showed that FAM84B was expressed mainly in luminal BC samples. Therefore, to determine the function of FAM84B in luminal BC cells, luminal BC cell lines with FAM84B knockout and overexpression were generated. In addition, the functions of FAM84B were evaluated in vitro (via cell proliferation, wound healing, colony formation and invasion assays) and in vivo (via a subcutaneous xenograft experiment), and the results showed that FAM84B regulated cell proliferation but not cell invasion. Furthermore, the results of RNA sequencing analysis in ZR-75-1 FAM84B knockout and FAM84B-overexpressing cells showed that FAM84B could affect the TNF signaling pathway. Subsequently, WB analysis of death receptor signaling and immunofluorescence (IF) analysis of NF-κB p65 localization revealed that FAM84B affected death receptor signaling and promoted NF-κB p65 nuclear entry. In conclusion, we found that FAM84B promotes luminal BC tumorigenesis through the activation of the NF-κB and death receptor signaling pathways. - Source: PubMed
Publication date: 2023/08/25
Zhang YanhuaYang Fang - Human endogenous retroviruses (HERVs) are LTR retrotransposons that are present in the human genome. Among them, members of the HERV-K (HML-2) group are suspected to play a role in the development of different types of cancer, including lung, ovarian, and prostate cancer, as well as leukemia. Acute myeloid leukemia (AML) is an important disease that causes 1% of cancer deaths in the United States and has a survival rate of 28.7%. Here, we describe a method for assessing the statistical association between HERV-K (HML-2) transposable element insertion polymorphisms (or TIPs) and AML, using whole-genome sequencing and read mapping using TIP_finder software. Our results suggest that 101 polymorphisms involving HERV-K (HML-2) elements were correlated with AML, with a percentage between 44.4 to 56.6%, most of which (70) were located in the region from 8q24.13 to 8q24.21. Moreover, it was found that the TRIB1, LRATD2, POU5F1B, MYC, PCAT1, PVT1, and CCDC26 genes could be displaced or fragmented by TIPs. Furthermore, a general method was devised to facilitate analysis of the correlation between transposable element insertions and specific diseases. Finally, although the relationship between HERV-K (HML-2) TIPs and AML remains unclear, the data reported in this study indicate a statistical correlation, as supported by the χ test with p-values < 0.05. - Source: PubMed
Publication date: 2023/03/29
Camargo-Forero NicolásOrozco-Arias SimonPerez Agudelo Juan MGuyot Romain - Kinetic parameters ( and ) derived from the Michaelis-Menten equation are widely used to characterize enzymes. / is considered the catalytic efficiency or substrate specificity of an enzyme toward its substrate. N-Myristoyltransferases (NMTs) catalyze the N-terminal glycine myristoylation of numerous eukaryotic proteins. Surprisingly, we find that in vitro human NMT1 can accept acetyl-CoA and catalyze acetylation with and values similar to that of myristoylation. However, when both acetyl-CoA and myristoyl-CoA are present in the reaction, NMT1 catalyzes almost exclusively myristoylation. This phenomenon is caused by the dramatically different binding affinities of NMT1 for myristoyl-CoA and acetyl-CoA (estimated of 14.7 nM and 10.1 μM, respectively). When both are present, NMT1 is essentially entirely bound by myristoyl-CoA and thus catalyzes myristoylation exclusively. The NMT1 example highlights the crucial role of binding affinity in determining the substrate specificity of enzymes, which in contrast to the traditionally held view in enzymology that the substrate specificity is defined by / values. This understanding readily explains the vast biological literature showing the coimmunoprecipitation of enzyme-substrate pairs for enzymes that catalyzes protein post-translational modifications (PTM), including phosphorylation, acetylation, and ubiquitination. Furthermore, this understanding allows the discovery of substrate proteins by identifying the interacting proteins of PTM enzymes, which we demonstrate by identifying three previously unknown substrate proteins (LRATD1, LRATD2, and ERICH5) of human NMT1/2 by mining available interactome data. - Source: PubMed
Publication date: 2021/11/29
Su DanKosciuk TatsianaYang MinPrice Ian RLin Hening - The fidelity of protein transport in the secretory pathway relies on the accurate sorting of proteins to their correct destinations. To deepen our understanding of the underlying molecular mechanisms, it is important to develop a robust approach to systematically reveal cargo proteins that depend on specific sorting machinery to be enriched into transport vesicles. Here, we used an in vitro assay that reconstitutes packaging of human cargo proteins into vesicles to quantify cargo capture. Quantitative mass spectrometry (MS) analyses of the isolated vesicles revealed cytosolic proteins that are associated with vesicle membranes in a GTP-dependent manner. We found that two of them, FAM84B (also known as LRAT domain containing 2 or LRATD2) and PRRC1, contain proline-rich domains and regulate anterograde trafficking. Further analyses revealed that PRRC1 is recruited to endoplasmic reticulum (ER) exit sites, interacts with the inner COPII coat, and its absence increases membrane association of COPII. In addition, we uncovered cargo proteins that depend on GTP hydrolysis to be captured into vesicles. Comparing control cells with cells depleted of the cargo receptors, SURF4 or ERGIC53, we revealed specific clients of each of these two export adaptors. Our results indicate that the vesicle formation assay in combination with quantitative MS analysis is a robust and powerful tool to uncover novel factors that mediate vesicular trafficking and to uncover cargo clients of specific cellular factors. - Source: PubMed
Huang YanYin HaidiLi BaiyingWu QianLiu YangPoljak KristinaMaldutyte JulijaTang XiaoWang MoWu ZhixiaoMiller Elizabeth AJiang LiwenYao Zhong-PingGuo Yusong - Metastatic and locally-advanced neuroendocrine neoplasms (aNEN) form clinically and genetically heterogeneous malignancies, characterized by distinct prognoses based upon primary tumor localization, functionality, grade, proliferation index and diverse outcomes to treatment. Here, we report the mutational landscape of 85 whole-genome sequenced aNEN. This landscape reveals distinct genomic subpopulations of aNEN based on primary localization and differentiation grade; we observe relatively high tumor mutational burdens (TMB) in neuroendocrine carcinoma (average 5.45 somatic mutations per megabase) with TP53, KRAS, RB1, CSMD3, APC, CSMD1, LRATD2, TRRAP and MYC as major drivers versus an overall low TMB in neuroendocrine tumors (1.09). Furthermore, we observe distinct drivers which are enriched in somatic aberrations in pancreatic (MEN1, ATRX, DAXX, DMD and CREBBP) and midgut-derived neuroendocrine tumors (CDKN1B). Finally, 49% of aNEN patients reveal potential therapeutic targets based upon actionable (and responsive) somatic aberrations within their genome; potentially directing improvements in aNEN treatment strategies. - Source: PubMed
Publication date: 2021/07/29
van Riet Jobvan de Werken Harmen J GCuppen EdwinEskens Ferry A L MTesselaar Margotvan Veenendaal Linde MKlümpen Heinz-JosefDercksen Marcus WValk Gerlof DLolkema Martijn PSleijfer StefanMostert Bianca