A piRNA-like small RNA interacts with and modulates p-ERM proteins in human somatic cells
Yuping Mei,
Yuyan Wang,
Priti Kumari,
Amol Carl Shetty,
David Clark,
Tyler Gable,
Alexander D. MacKerell,
Mark Z. Ma,
David J. Weber,
Austin J. Yang,
Martin J. Edelman and
Li Mao ()
Additional contact information
Yuping Mei: University of Maryland School of Dentistry
Yuyan Wang: University of Maryland School of Dentistry
Priti Kumari: Institute for Genome Sciences, University of Maryland School of Medicine
Amol Carl Shetty: Institute for Genome Sciences, University of Maryland School of Medicine
David Clark: University of Maryland School of Dentistry
Tyler Gable: University of Maryland School of Dentistry
Alexander D. MacKerell: Computer-Aided Drug Design Center, University of Maryland School of Pharmacy
Mark Z. Ma: University of Maryland School of Dentistry
David J. Weber: Marlene and Stewart Greenebaum Cancer Center, University of Maryland
Austin J. Yang: Marlene and Stewart Greenebaum Cancer Center, University of Maryland
Martin J. Edelman: Marlene and Stewart Greenebaum Cancer Center, University of Maryland
Li Mao: University of Maryland School of Dentistry
Nature Communications, 2015, vol. 6, issue 1, 1-12
Abstract:
Abstract PIWI-interacting RNAs (piRNAs) are thought to silence transposon and gene expression during development. However, the roles of piRNAs in somatic tissues are largely unknown. Here we report the identification of 555 piRNAs in human lung bronchial epithelial (HBE) and non-small cell lung cancer (NSCLC) cell lines, including 295 that do not exist in databases termed as piRNA-like sncRNAs or piRNA-Ls. Distinctive piRNA/piRNA-L expression patterns are observed between HBE and NSCLC cells. piRNA-like-163 (piR-L-163), the top downregulated piRNA-L in NSCLC cells, binds directly to phosphorylated ERM proteins (p-ERM), which is dependent on the central part of UUNNUUUNNUU motif in piR-L-163 and the RRRKPDT element in ERM. The piR-L-163/p-ERM interaction is critical for p-ERM’s binding capability to filamentous actin (F-actin) and ERM-binding phosphoprotein 50 (EBP50). Thus, piRNA/piRNA-L may play a regulatory role through direct interaction with proteins in physiological and pathophysiological conditions.
Date: 2015
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8316
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DOI: 10.1038/ncomms8316
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