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The SMN Tudor SIM-like domain is key to SmD1 and coilin interactions and to cajal body biogenesis

AutorTapia, Olga; Lafarga, Vanesa ; Bengoechea, Rocio; Palanca, Ana; Lafarga, Miguel; Berciano, María T.
Fecha de publicación2014
EditorCompany of Biologists
CitaciónJournal of Cell Science 127: 939- 946 (2014)
ResumenCajal bodies (CBs) are nuclear organelles involved in the maturation of spliceosomal small nuclear ribonucleoproteins (snRNPs). They concentrate coilin, snRNPs and the survival motor neuron protein (SMN). Dysfunction of CB assembly occurs in spinal muscular atrophy (SMA). Here, we demonstrate that SMN is a SUMO1 target that has a small ubiquitin-related modifier (SUMO)-interacting motif (SIM)-like motif in the Tudor domain. The expression of SIM-like mutant constructs abolishes the interaction of SMN with the spliceosomal SmD1 (also known as SNRPD1), severely decreases SMN-coilin interaction and prevents CB assembly. Accordingly, the SMN SIM-like-mediated interactions are important for CB biogenesis and their dysfunction can be involved in SMA pathophysiology. © 2014. Published by The Company of Biologists Ltd.
URIhttp://hdl.handle.net/10261/126345
DOI10.1242/jcs.138537
Identificadoresdoi: 10.1242/jcs.138537
issn: 0021-9533
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