Human <scp>DND1‐RRM2</scp> forms a non‐canonical domain swapped dimer

Kumari, Pooja; Bhavesh, Neel Sarovar

doi:10.1002/pro.4083

Cited by 5 publications

(1 citation statement)

References 47 publications

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“…Whether the different reported functions of DND1 are species-specific also remains to be clarified. A recent study revealed an interesting 3D domain swapped dimerization of the DND1-RRM2 domain [40], which increases surface area for multimeric interactions and may allow DND1 to exert different functions in different context. Further investigations are warranted to elucidate the mechanisms and causes underlying the multifaceted roles of DND1.…”

Section: Other Molecular Functions Of Dnd1mentioning

confidence: 99%

The Role of DND1 in Cancers

Zhang

Godavarthi

Williams-Villalobo

et al. 2021

Cancers

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The Ter mutation in Dead-End 1 (Dnd1), Dnd1Ter, which leads to a premature stop codon, has been determined to be the cause for primordial germ cell deficiency, accompanied with a high incidence of congenital testicular germ cell tumors (TGCTs) or teratomas in the 129/Sv-Ter mice. As an RNA-binding protein, DND1 can bind the 3′-untranslated region (3′-UTR) of mRNAs and function in translational regulation. DND1 can block microRNA (miRNA) access to the 3′-UTR of target mRNAs, thus inhibiting miRNA-mediated mRNA degradation and up-regulating translation or can also function to degrade or repress mRNAs. Other mechanisms of DND1 activity include promoting translation initiation and modifying target protein activity. Although Dnd1Ter mutation causes spontaneous TGCT only in male 129 mice, it can also cause ovarian teratomas in mice when combined with other genetic defects or cause germ cell teratomas in both genders in the WKY/Ztm rat strain. Furthermore, studies on human cell lines, patient cancer tissues, and the use of human cancer genome analysis indicate that DND1 may possess either tumor-suppressive or -promoting functions in a variety of somatic cancers. Here we review the involvement of DND1 in cancers, including what appears to be its emerging role in somatic cancers.

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Section: Other Molecular Functions Of Dnd1mentioning

confidence: 99%

The Role of DND1 in Cancers

Zhang

Godavarthi

Williams-Villalobo

et al. 2021

Cancers

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Human DND1‐RRM2 forms a non‐canonical domain swapped dimer

Kumari

Bhavesh

2021

Protein Science

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RNA recognition motif (RRM) being the most abundant RNA binding domain in eukaryotes, is a major player in cellular regulation. Several variations in the canonical βαββαβ topology have been observed. We have determined the 2.3 Å crystal structure of the human DND1-RRM2 domain. The structure revealed an interesting non-canonical RRM fold, which is maintained by the formation of a 3D domain swapped dimer between β 1 and β 4 strands across protomers.We have delineated the structural basis of the stable domain swapped dimer formation using the residue level dynamics of protein explored by NMR spectroscopy and MD simulations. Our structural and dynamics studies substantiate major determinants and molecular basis for domain swapped dimerization observed in the RRM domain.

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Biochemical and subcellular characterization of a squid hnRNPA/B-like protein 2 in osmotic stress activated cells reflects molecular properties conserved in this protein family

Lopes

Lico

2022

Mol Biol Rep

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In previous works, we characterized a novel, strongly basic, squid hnRNPA/B-like Protein 2 in presynaptic terminals of squid neurons. Here, we show that squid hnRNPA/B-like Protein 2 are exclusively nuclear localization and relocated to cytoplasmic granules containing hnRNPA1 and Poly-A binding protein-1 (PABP-1) when the cells are treated with sorbitol. Also, we show an interaction of hnRNPA/B like Protein 2 with squid RNA, its interfered with dynamic of formation of hnRNPA/B like Protein 2 dimers, whereas possibly involved disulfide bounds and postranslations modification in a distinct stage of dimers formation. An understanding of the molecular and biochemical mechanisms involved in the stability of the dimeric form, and the regulation of the transition between monomeric and dimeric forms may bring insights into evolution of several neurodegenerative diseases.

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Human DND1‐RRM2 forms a non‐canonical domain swapped dimer

Cited by 5 publications

References 47 publications

The Role of DND1 in Cancers

The Role of DND1 in Cancers

Human DND1‐RRM2 forms a non‐canonical domain swapped dimer

Biochemical and subcellular characterization of a squid hnRNPA/B-like protein 2 in osmotic stress activated cells reflects molecular properties conserved in this protein family

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