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Chaolin Zhang on Muck Rack

Chaolin Zhang

As seen in: Nature, MDPI, Science Magazine, BioRxiv, Cell Press, JNeurosci, Scientific Research Publishing (SCIRP), TechTrends
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Articles

Exon inclusion signatures enable accurate estimation of splicing factor activity

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By Miquel Anglada-Girotto, Carolina Segura-Morales, Daniel F. Moakley, Chaolin Zhang, Samuel Miravet-Verde, Andrea Califano, Luis Serrano
| Nature Verified
Abstract Splicing factors control exon inclusion in messenger RNAs, shaping transcriptome and proteome diversity. Their catalytic activity is regulated by multiple layers, making single-omic measurements on their own fall short in identifying which splicing factors underlie a phenotype. Here, we posit that splicing factor activity, defined as a splicing factor’s ability to modulate exon inclusion, can be estimated from changes in exon inclusion signatures.
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A neuron type-specific microexon in Ank3/ankyrin-G modulates calcium activity and neuronal excitability - Nature Communications

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By Shah Alam, Georgia Dermentzaki, Miao Li Verified, Ruizhi Wang, Melissa Campbell, Ilaria Balbo, Brittany Phillips, Min Li, Jessica Estrada Verified, Marianna Zazhytska, Yow-Tyng Yeh, Lia Min, Elizabeth E Rafikian, Elizabeth Rhiannon Valenzuela, Brian Joseph, Dmytro Ustianenko, Helene C. Lovett, Huijuan Feng, Xiaojian Wang, Susan Brenner-Morton, Chyuan-Sheng Lin, Clarissa L. Waites, Hynek Wichterle, Lizhen Chen, Edmund Au, Marko Jovanovic Verified, Stavros Lomvardas, Paul Jenkins, Rui Yang, Sheng-Han Kuo, Yueqing Peng, Guang Yang, Neil Harrison, Chaolin Zhang, David Cabrera-Garcia
| Nature Verified
Abstract Recent studies have revealed many alternative exons differentially spliced across diverse neuron types in the mammalian brain, but their links to neuronal physiology remain unclear. Here we characterize a deeply conserved microexon E35a in Ank3 encoding ankyrin-G (AnkG), a multifaceted adaptor protein best known as a master organizer of the axon initial segment (AIS) and as a leading genetic risk factor for bipolar disorder.
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TDP-43-dependent mis-splicing of KCNQ2 triggers intrinsic neuronal hyperexcitability in ALS/FTD - Nature Neuroscience

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By Brian Joseph, Kelly Marshall, Peter Harley, Wanhao Chi, Mercedes Prudencio, Dina Simkin, Tzu-Ting Kao, Matthew J. Keuss, Simone Barattucci, Puja R Mehta, Jonathan Lee, Marcel F. Leyton-Jaimes, Eleonora Aronica, Brian J. Wainger, Dennis W. Dickson, Chaolin Zhang, Hynek Wichterle, Jonathan Watts, Pietro Fratta, Kevin Eggan
| Nature Verified
Abstract Motor neuron hyperexcitability is a broadly observed yet poorly understood feature of amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Nuclear depletion and cytoplasmic aggregation of the RNA splicing protein TAR DNA-binding protein 43 (TDP-43) are observed in most ALS and FTD patients. Here we show that TDP-43 dysfunction causes mis-splicing of KCNQ2, which encodes a voltage-gated potassium channel (Kv7.2) that regulates neuronal excitability.
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