ArticleProtein science : a publication of the Protein Society2009
Solution structure of the RNA binding domain in the human muscleblind-like protein 2.
Article in Protein science : a publication of the Protein Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 22 citations in OpenAlex.
- MBNL2 enhances cisplatin resistance by regulating apoptosis in ovarian cancer cells.BMB reports · 2025Article
- Functions of the Muscleblind-like protein family and their role in disease.Cell communication and signaling : CCS · 2025Review
- Cognate RNA-Binding Modes by the Alternative-Splicing Regulator MBNL1 Inferred from Molecular Dynamics.International journal of molecular sciences · 2022Article
- MBNL2 Regulates DNA Damage Response via Stabilizing p21.International journal of molecular sciences · 2021Article
- MBNL splicing activity depends on RNA binding site structural context.Nucleic acids research · 2018Article
- Structural Basis for Interaction of the Tandem Zinc Finger Domains of Human Muscleblind with Cognate RNA from Human Cardiac Troponin T.Biochemistry · 2017Article
- Mechanistic determinants of MBNL activity.Nucleic acids research · 2016Article
- Nuclear retention of full-length HTT RNA is mediated by splicing factors MBNL1 and U2AF65.Scientific reports · 2015Article
- Creatine kinase B is necessary to limit myoblast fusion during myogenesis.American journal of physiology. Cell physiology · 2015Article
- Dissecting domains necessary for activation and repression of splicing by Muscleblind-like protein 1.BMC molecular biology · 2013Article
- Insulin receptor isoform switching in intestinal stem cells, progenitors, differentiated lineages and tumors: evidence that IR-B limits proliferation.Journal of cell science · 2013Article
- MBNL1 and PTB cooperate to repress splicing of Tpm1 exon 3.Nucleic acids research · 2013Article
- A CCCH-type zinc finger nucleic acid-binding protein quantitatively confers resistance against rice bacterial blight disease.Plant physiology · 2012Article
- The four Zn fingers of MBNL1 provide a flexible platform for recognition of its RNA binding elements.BMC molecular biology · 2011Article
- Identification of MBNL1 and MBNL3 domains required for splicing activation and repression.Nucleic acids research · 2011Article
- RNA-binding protein Muscleblind-like 3 (MBNL3) disrupts myocyte enhancer factor 2 (Mef2) {beta}-exon splicing.The Journal of biological chemistry · 2010Article
- Aberrant alternative splicing and extracellular matrix gene expression in mouse models of myotonic dystrophy.Nature structural & molecular biology · 2010Article
- Molecular geometry of CsrA (RsmA) binding to RNA and its implications for regulated expression.Journal of molecular biology · 2009Article
- Muscleblind-like 2: circadian expression in the mammalian pineal gland is controlled by an adrenergic-cAMP mechanism.Journal of neurochemistry · 2009Article
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Authors and funding
20 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The muscleblind-like (MBNL) proteins 1, 2, and 3, which contain four CCCH zinc finger motifs (ZF1-4), are involved in the differentiation of muscle inclusion by controlling the splicing patterns of several pre-mRNAs. Especially, MBNL1 plays a crucial role in myotonic dystrophy. The CCCH zinc finger is a sequence motif found in many RNA binding proteins and is suggested to play an important role in the recognition of RNA molecules. Here, we solved the solution structures of both tandem zinc finger (TZF) motifs, TZF12 (comprising ZF1 and ZF2) and TZF34 (ZF3 and ZF4), in MBNL2 from Homo sapiens. In TZF12 of MBNL2, ZF1 and ZF2 adopt a similar fold, as reported previously for the CCCH-type zinc fingers in the TIS11d protein. The linker between ZF1 and ZF2 in MBNL2 forms an antiparallel beta-sheet with the N-terminal extension of ZF1. Furthermore, ZF1 and ZF2 in MBNL2 interact with each other through hydrophobic interactions. Consequently, TZF12 forms a single, compact global fold, where ZF1 and ZF2 are approximately symmetrical about the C2 axis. The structure of the second tandem zinc finger (TZF34) in MBNL2 is similar to that of TZF12. This novel three-dimensional structure of the TZF domains in MBNL2 provides a basis for functional studies of the CCCH-type zinc finger motifs in the MBNL protein family.
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