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000139338 0247_ $$2doi$$a10.1016/j.yexcr.2017.04.024
000139338 0247_ $$2pmid$$apmid:28442266
000139338 0247_ $$2ISSN$$a0014-4827
000139338 0247_ $$2ISSN$$a1090-2422
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000139338 037__ $$aDZNE-2020-05660
000139338 041__ $$aEnglish
000139338 082__ $$a570
000139338 1001_ $$aJules, Felix$$b0
000139338 245__ $$aCLN5 is cleaved by members of the SPP/SPPL family to produce a mature soluble protein.
000139338 260__ $$aOrlando, Fla.$$bAcademic Press$$c2017
000139338 264_1 $$2Crossref$$3print$$bElsevier BV$$c2017-08-01
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000139338 520__ $$aThe Neuronal ceroid lipofuscinoses (NCLs) are a group of recessive disorders of childhood with overlapping symptoms including vision loss, ataxia, cognitive regression and premature death. 14 different genes have been linked to NCLs (CLN1-CLN14), but the functions of the proteins encoded by the majority of these genes have not been fully elucidated. Mutations in the CLN5 gene are responsible for the Finnish variant late-infantile form of NCL (Finnish vLINCL). CLN5 is translated as a 407 amino acid transmembrane domain containing protein that is heavily glycosylated, and subsequently cleaved into a mature soluble protein. Functionally, CLN5 is implicated in the recruitment of the retromer complex to endosomes, which is required to sort the lysosomal sorting receptors from endosomes to the trans-Golgi network. The mechanism that processes CLN5 into a mature soluble protein is currently not known. Herein, we demonstrate that CLN5 is initially translated as a type II transmembrane protein and subsequently cleaved by SPPL3, a member of the SPP/SPPL intramembrane protease family, into a mature soluble protein consisting of residues 93-407. The remaining N-terminal fragment is then cleaved by SPPL3 and SPPL2b and degraded in the proteasome. This work further characterizes the biology of CLN5 in the hopes of identifying a novel therapeutic strategy for affected children.
000139338 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
000139338 542__ $$2Crossref$$i2017-08-01$$uhttps://www.elsevier.com/tdm/userlicense/1.0/
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000139338 650_7 $$2NLM Chemicals$$aCLN5 protein, human
000139338 650_7 $$2NLM Chemicals$$aMembrane Proteins
000139338 650_7 $$0EC 3.4.23.-$$2NLM Chemicals$$aAspartic Acid Endopeptidases
000139338 650_2 $$2MeSH$$aLysosome-Associated Membrane Glycoproteins
000139338 650_2 $$2MeSH$$aAspartic Acid Endopeptidases: metabolism
000139338 650_2 $$2MeSH$$aCell Line
000139338 650_2 $$2MeSH$$aEndosomes: metabolism
000139338 650_2 $$2MeSH$$aHumans
000139338 650_2 $$2MeSH$$aLysosomes: metabolism
000139338 650_2 $$2MeSH$$aMembrane Proteins: metabolism
000139338 650_2 $$2MeSH$$aNeuronal Ceroid-Lipofuscinoses: metabolism
000139338 650_2 $$2MeSH$$aProtein Transport
000139338 650_2 $$2MeSH$$aSolubility
000139338 650_2 $$2MeSH$$atrans-Golgi Network: metabolism
000139338 7001_ $$aSauvageau, Etienne$$b1
000139338 7001_ $$aDumaresq-Doiron, Karine$$b2
000139338 7001_ $$aMazzaferri, Javier$$b3
000139338 7001_ $$aHaug-Kröper, Martina$$b4
000139338 7001_ $$0P:(DE-2719)2000007$$aFluhrer, Regina$$b5$$udzne
000139338 7001_ $$aCostantino, Santiago$$b6
000139338 7001_ $$0P:(DE-HGF)0$$aLefrancois, Stephane$$b7$$eCorresponding author
000139338 77318 $$2Crossref$$3journal-article$$a10.1016/j.yexcr.2017.04.024$$b : Elsevier BV, 2017-08-01$$n1$$p40-50$$tExperimental Cell Research$$v357$$x0014-4827$$y2017
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