Home > Publications Database > CLN5 is cleaved by members of the SPP/SPPL family to produce a mature soluble protein. > print

001     139338
005     20240321220612.0
024 7 _ |a 10.1016/j.yexcr.2017.04.024
|2 doi
024 7 _ |a pmid:28442266
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024 7 _ |a 0014-4827
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024 7 _ |a 1090-2422
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037 _ _ |a DZNE-2020-05660
041 _ _ |a English
082 _ _ |a 570
100 1 _ |a Jules, Felix
|b 0
245 _ _ |a CLN5 is cleaved by members of the SPP/SPPL family to produce a mature soluble protein.
260 _ _ |a Orlando, Fla.
|c 2017
|b Academic Press
264 _ 1 |3 print
|2 Crossref
|b Elsevier BV
|c 2017-08-01
336 7 _ |a article
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336 7 _ |a ARTICLE
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336 7 _ |a Journal Article
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520 _ _ |a The 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.
536 _ _ |a 342 - Disease Mechanisms and Model Systems (POF3-342)
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542 _ _ |i 2017-08-01
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|u https://www.elsevier.com/tdm/userlicense/1.0/
588 _ _ |a Dataset connected to CrossRef, PubMed,
650 _ 7 |a CLN5 protein, human
|2 NLM Chemicals
650 _ 7 |a Membrane Proteins
|2 NLM Chemicals
650 _ 7 |a Aspartic Acid Endopeptidases
|0 EC 3.4.23.-
|2 NLM Chemicals
650 _ 2 |a Lysosome-Associated Membrane Glycoproteins
|2 MeSH
650 _ 2 |a Aspartic Acid Endopeptidases: metabolism
|2 MeSH
650 _ 2 |a Cell Line
|2 MeSH
650 _ 2 |a Endosomes: metabolism
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Lysosomes: metabolism
|2 MeSH
650 _ 2 |a Membrane Proteins: metabolism
|2 MeSH
650 _ 2 |a Neuronal Ceroid-Lipofuscinoses: metabolism
|2 MeSH
650 _ 2 |a Protein Transport
|2 MeSH
650 _ 2 |a Solubility
|2 MeSH
650 _ 2 |a trans-Golgi Network: metabolism
|2 MeSH
700 1 _ |a Sauvageau, Etienne
|b 1
700 1 _ |a Dumaresq-Doiron, Karine
|b 2
700 1 _ |a Mazzaferri, Javier
|b 3
700 1 _ |a Haug-Kröper, Martina
|b 4
700 1 _ |a Fluhrer, Regina
|0 P:(DE-2719)2000007
|b 5
|u dzne
700 1 _ |a Costantino, Santiago
|b 6
700 1 _ |a Lefrancois, Stephane
|0 P:(DE-HGF)0
|b 7
|e Corresponding author
773 1 8 |a 10.1016/j.yexcr.2017.04.024
|b : Elsevier BV, 2017-08-01
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|t Experimental Cell Research
|v 357
|y 2017
|x 0014-4827
773 _ _ |a 10.1016/j.yexcr.2017.04.024
|g Vol. 357, no. 1, p. 40 - 50
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910 1 _ |a Deutsches Zentrum für Neurodegenerative Erkrankungen
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