Ask about this productRelated genes to: ANKS3 antibody
- Gene:
- ANKS3 NIH gene
- Name:
- ankyrin repeat and sterile alpha motif domain containing 3
- Previous symbol:
- -
- Synonyms:
- KIAA1977, FLJ32345, FLJ32767
- Chromosome:
- 16p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2006-02-17
- Date modifiied:
- 2014-11-19
Related products to: ANKS3 antibody
Related articles to: ANKS3 antibody
- In vertebrates, left-right (LR) asymmetry is specified by asymmetric decay of messenger RNA (mRNA) mediated by the recruitment of the BicC family RNA binding protein 1 (Bicc1). Besides regulating organ laterality, Bicc1 is required to prevent cystic dilations in renal tubules and in pancreatic and bile ducts. However, validated target mRNAs are sparse in number, and how their binding to Bicc1 is regulated remains poorly understood. Bicc1 recruitment to transcripts requires a conserved AGACGUGAC motif in the 3'UTR. Here, we report an N-methyladenosine (mA) in this sequence that disrupts binding to Bicc1 K homology (KH) domains in vitro, in stark contrast to IGF2BPs and FMR1, where mA promotes RNA recognition by KH domains. We discuss the possible implications of this finding for LR axis formation and for a related role of Bicc1 in regulating specific target mRNAs in the kidney. - Source: PubMed
Publication date: 2025/09/16
Rothé BenjaminMendel MateuszFortier SimonConstam Daniel B - Organ laterality of vertebrates is specified by accelerated asymmetric decay of Dand5 mRNA mediated by Bicaudal-C1 (Bicc1) on the left side, but whether binding of this or any other mRNA to Bicc1 can be regulated is unknown. Here, we found that a CRISPR-engineered truncation in ankyrin and sterile alpha motif (SAM)-containing 3 (ANKS3) leads to symmetric mRNA decay mediated by the Bicc1-interacting Dand5 3' UTR. AlphaFold structure predictions of protein complexes and their biochemical validation by in vitro reconstitution reveal a novel interaction of the C-terminal coiled coil domain of ANKS3 with Bicc1 that inhibits binding of target mRNAs, depending on the conformation of ANKS3 and its regulation by ANKS6. The dual regulation of RNA binding by mutually opposing structured protein domains in this multivalent protein network emerges as a novel mechanism linking associated laterality defects and possibly other ciliopathies to perturbed dynamics in Bicc1 ribonucleoparticle (RNP) formation. - Source: PubMed
Publication date: 2023/09/21
Rothé BenjaminIkawa YayoiZhang ZhidianKatoh Takanobu AKajikawa ErikoMinegishi KatsuraXiaorei SaiFortier SimonDal Peraro MatteoHamada HiroshiConstam Daniel B - The growing number of diseases linked to aberrant phase transitioning of ribonucleoproteins highlights the need to uncover how the interplay between multivalent protein and RNA interactions is regulated. Cytoplasmic granules of the RNA binding protein Bicaudal-C (Bicc1) are regulated by the ciliopathy proteins ankyrin (ANK) and sterile alpha motif (SAM) domain-containing ANKS3 and ANKS6, but whether and how target mRNAs are affected is unknown. Here, we show that head-to-tail polymers of Bicc1 nucleated by its SAM domain are interconnected by K homology (KH) domains in a protein meshwork that mediates liquid-to-gel transitioning of client transcripts. Moreover, while the dispersion of these granules by ANKS3 concomitantly released bound mRNAs, co-recruitment of ANKS6 by ANKS3 reinstated Bicc1 condensation and ribonucleoparticle assembly. RNA-independent Bicc1 polymerization and its dual regulation by ANKS3 and ANKS6 represent a new mechanism to couple the reversible immobilization of client mRNAs to controlled protein phase transitioning between distinct metastable states. - Source: PubMed
Publication date: 2023/05/11
Rothé BenjaminFortier SimonGagnieux CélineSchmuziger CélineConstam Daniel B - Suboptimal nutrition in pregnancy is associated with worse offspring cardiometabolic health. DNA methylation may be an underlying mechanism. We meta-analyzed epigenome-wide association studies (EWAS) of maternal dietary glycemic index and load with cord blood DNA methylation. - Source: PubMed
Küpers Leanne KFernández-Barrés SílviaMancano GiuliaJohnson LauraOtt RaffaelVioque JesusColombo MarcoLandgraf KathrinTobi Elmar WKörner AntjeGaillard Romyde Vries Jeanne H MJaddoe Vincent W VVrijheid MartineSharp Gemma CFelix Janine F - Mutations of cilia-associated molecules cause multiple developmental defects that are collectively termed ciliopathies. However, several ciliary proteins, involved in gating access to the cilium, also assume localizations at other cellular sites including the nucleus, where they participate in DNA damage responses to maintain tissue integrity. Molecular insight into how these molecules execute such diverse functions remains limited. A mass spectrometry screen for ANKS6-interacting proteins suggested an involvement of ANKS6 in RNA processing and/or binding. Comparing the RNA-binding properties of the known RNA-binding protein BICC1 with the three ankyrin-repeat proteins ANKS3, ANKS6 (NPHP16) and INVERSIN (NPHP2) confirmed that certain nephronophthisis (NPH) family members can interact with RNA molecules. We also observed that BICC1 and INVERSIN associate with stress granules in response to translational inhibition. Furthermore, BICC1 recruits ANKS3 and ANKS6 into TIA-1-positive stress granules after exposure to hippuristanol. Our findings uncover a novel function of NPH family members, and provide further evidence that NPH family members together with BICC1 are involved in stress responses to maintain tissue and organ integrity. - Source: PubMed
Publication date: 2020/09/29
Estrada Mallarino LuisaEngel ChristinaIlık İbrahim AvşarMaticzka DanielHeyl FlorianMüller BarbaraYakulov Toma ADengjel JörnBackofen RolfAkhtar AsifaWalz Gerd