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SAM68 regulates neuronal activity-dependent alternative splicing of neurexin-1

SAM68 regulates neuronal activity-dependent alternative splicing of neurexin-1

Cell 147(7): 1601-1614

ISSN/ISBN: 0092-8674

PMID: 22196734

DOI: 10.1016/j.cell.2011.11.028

The assembly of synapses and neuronal circuits relies on an array of molecular recognition events and their modification by neuronal activity. Neurexins are a highly polymorphic family of synaptic receptors diversified by extensive alternative splicing. Neurexin variants exhibit distinct isoform-specific biochemical interactions and synapse assembly functions, but the mechanisms governing splice isoform choice are not understood. We demonstrate thatNrxn1alternative splicing is temporally and spatially controlled in the mouse brain. Neuronal activity triggers a shift inNrxn1splice isoform choice via calcium/calmodulin-dependent kinase IV signaling. Activity-dependent alternative splicing ofNrxn1requires the KH-domain RNA-binding protein SAM68 that associates with RNA response elements in theNrxn1pre-mRNA. Our findings uncover SAM68 as a key regulator of dynamic control ofNrxn1molecular diversity and activity-dependent alternative splicing in the central nervous system.Neurexin splice variants engage in an adhesive code via postsynaptic receptors Alternative splicing of neurexins is regulated by neuronal activity and CaMKIV SAM68 interacts with response elements in neurexin-1 pre-mRNA SAM68 is essential for activity-dependent alternative splicing of neurexin-1.

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Accession: 055630117

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