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000131785 0247_ $$2doi$$a10.1007/s00018-017-2638-2
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000131785 0247_ $$2ISSN$$a0014-4754
000131785 0247_ $$2ISSN$$a1420-682X
000131785 0247_ $$2ISSN$$a1420-9071
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000131785 037__ $$aDKFZ-2018-00082
000131785 041__ $$aeng
000131785 082__ $$a570
000131785 1001_ $$aLafarga, Vanesa$$b0
000131785 245__ $$aCBP-mediated SMN acetylation modulates Cajal body biogenesis and the cytoplasmic targeting of SMN.
000131785 260__ $$aBasel$$bBirkhäuser$$c2018
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000131785 520__ $$aThe survival of motor neuron (SMN) protein plays an essential role in the biogenesis of spliceosomal snRNPs and the molecular assembly of Cajal bodies (CBs). Deletion of or mutations in the SMN1 gene cause spinal muscular atrophy (SMA) with degeneration and loss of motor neurons. Reduced SMN levels in SMA lead to deficient snRNP biogenesis with consequent splicing pathology. Here, we demonstrate that SMN is a novel and specific target of the acetyltransferase CBP (CREB-binding protein). Furthermore, we identify lysine (K) 119 as the main acetylation site in SMN. Importantly, SMN acetylation enhances its cytoplasmic localization, causes depletion of CBs, and reduces the accumulation of snRNPs in nuclear speckles. In contrast, the acetylation-deficient SMNK119R mutant promotes formation of CBs and a novel category of promyelocytic leukemia (PML) bodies enriched in this protein. Acetylation increases the half-life of SMN protein, reduces its cytoplasmic diffusion rate and modifies its interactome. Hence, SMN acetylation leads to its dysfunction, which explains the ineffectiveness of HDAC (histone deacetylases) inhibitors in SMA therapy despite their potential to increase SMN levels.
000131785 536__ $$0G:(DE-HGF)POF3-311$$a311 - Signalling pathways, cell and tumor biology (POF3-311)$$cPOF3-311$$fPOF III$$x0
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000131785 7001_ $$00000-0002-0802-7975$$aTapia, Olga$$b1
000131785 7001_ $$0P:(DE-He78)0ccaac599df473c058110b44c7b292c0$$aSharma, Sahil$$b2$$udkfz
000131785 7001_ $$aBengoechea, Rocio$$b3
000131785 7001_ $$0P:(DE-HGF)0$$aStoecklin, Georg$$b4
000131785 7001_ $$aLafarga, Miguel$$b5
000131785 7001_ $$aBerciano, Maria T$$b6
000131785 773__ $$0PERI:(DE-600)1458497-9$$a10.1007/s00018-017-2638-2$$gVol. 75, no. 3, p. 527 - 546$$n3$$p527 - 546$$tCellular and molecular life sciences$$v75$$x1420-9071$$y2018
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000131785 9141_ $$y2018
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