Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease

Peters J, Rittger A, Weisner R, Knabbe J, Zunke F, Rothaug M, Damme M, Berkovic SF, Blanz J, Saftig P, Schwake M (2015)
Biochemical and Biophysical Research Communications 457(3): 334-340.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
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Autor*in
Peters, Judith; Rittger, Andrea; Weisner, Rebecca; Knabbe, Johannes; Zunke, Friederike; Rothaug, Michelle; Damme, Markus; Berkovic, Samuel F.; Blanz, Judith; Saftig, Paul; Schwake, MichaelUniBi
Abstract / Bemerkung
The lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) has been identified as a receptor for enterovirus 71 uptake and mannose-6-phosphate-independent lysosomal trafficking of the acid hydrolase beta-glucocerebrosidase. Here we show that LIMP-2 undergoes proteolytic cleavage mediated by lysosomal cysteine proteases. Heterologous expression and in vitro studies suggest that cathepsin-F is mainly responsible for the lysosomal processing of wild-type LIMP-2. Furthermore, examination of purified lysosomes revealed that LIMP-2 undergoes proteolysis in vivo. Mutations in the gene encoding cathepsin-F (CTSF) have recently been associated with type-B-Kufs-disease, an adult form of neuronal ceroid-lipofuscinosis. In this study we show that disease-causing cathepsin-F mutants fail to cleave LIMP-2. Our findings provide evidence that LIMP-2 represents an in vivo substrate of cathepsin-F with relevance for understanding the pathophysiology of type-B-Kufs-disease. (C) 2015 Elsevier Inc. All rights reserved.
Stichworte
ceroid-lipofuscinosis; Neuronal; Lysosomal storage disease; Cathepsin-F; LIMP-2; Kufs disease
Erscheinungsjahr
2015
Zeitschriftentitel
Biochemical and Biophysical Research Communications
Band
457
Ausgabe
3
Seite(n)
334-340
ISSN
0006-291X
Page URI
https://pub.uni-bielefeld.de/record/2731248

Zitieren

Peters J, Rittger A, Weisner R, et al. Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease. Biochemical and Biophysical Research Communications. 2015;457(3):334-340.
Peters, J., Rittger, A., Weisner, R., Knabbe, J., Zunke, F., Rothaug, M., Damme, M., et al. (2015). Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease. Biochemical and Biophysical Research Communications, 457(3), 334-340. doi:10.1016/j.bbrc.2014.12.111
Peters, J., Rittger, A., Weisner, R., Knabbe, J., Zunke, F., Rothaug, M., Damme, M., Berkovic, S. F., Blanz, J., Saftig, P., et al. (2015). Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease. Biochemical and Biophysical Research Communications 457, 334-340.
Peters, J., et al., 2015. Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease. Biochemical and Biophysical Research Communications, 457(3), p 334-340.
J. Peters, et al., “Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease”, Biochemical and Biophysical Research Communications, vol. 457, 2015, pp. 334-340.
Peters, J., Rittger, A., Weisner, R., Knabbe, J., Zunke, F., Rothaug, M., Damme, M., Berkovic, S.F., Blanz, J., Saftig, P., Schwake, M.: Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease. Biochemical and Biophysical Research Communications. 457, 334-340 (2015).
Peters, Judith, Rittger, Andrea, Weisner, Rebecca, Knabbe, Johannes, Zunke, Friederike, Rothaug, Michelle, Damme, Markus, Berkovic, Samuel F., Blanz, Judith, Saftig, Paul, and Schwake, Michael. “Lysosomal integral membrane protein type-2 (LIMP-2/SCARB2) is a substrate of cathepsin-F, a cysteine protease mutated in type-B-Kufs-disease”. Biochemical and Biophysical Research Communications 457.3 (2015): 334-340.

5 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Emerging new roles of the lysosome and neuronal ceroid lipofuscinoses.
Mukherjee AB, Appu AP, Sadhukhan T, Casey S, Mondal A, Zhang Z, Bagh MB., Mol Neurodegener 14(1), 2019
PMID: 30651094
Alu-Derived Alternative Splicing Events Specific to Macaca Lineages in CTSF Gene.
Lee JR, Park SJ, Kim YH, Choe SH, Cho HM, Lee SR, Kim SU, Kim JS, Sim BW, Song BS, Jeong KJ, Lee Y, Jin YB, Kang P, Huh JW, Chang KT., Mol Cells 40(2), 2017
PMID: 28196413
The Multifaceted Role of the Lysosomal Protease Cathepsins in Kidney Disease.
Cocchiaro P, De Pasquale V, Della Morte R, Tafuri S, Avallone L, Pizard A, Moles A, Pavone LM., Front Cell Dev Biol 5(), 2017
PMID: 29312937
Intramembrane proteolysis within lysosomes.
Schröder B, Saftig P., Ageing Res Rev 32(), 2016
PMID: 27143694
Mannose 6-phosphate-independent Lysosomal Sorting of LIMP-2.
Blanz J, Zunke F, Markmann S, Damme M, Braulke T, Saftig P, Schwake M., Traffic 16(10), 2015
PMID: 26219725

40 References

Daten bereitgestellt von Europe PubMed Central.

LIMP-2 is a receptor for lysosomal mannose-6-phosphate-independent targeting of beta-glucocerebrosidase.
Reczek D, Schwake M, Schroder J, Hughes H, Blanz J, Jin X, Brondyk W, Van Patten S, Edmunds T, Saftig P., Cell 131(4), 2007
PMID: 18022370
Structure of LIMP-2 provides functional insights with implications for SR-BI and CD36.
Neculai D, Schwake M, Ravichandran M, Zunke F, Collins RF, Peters J, Neculai M, Plumb J, Loppnau P, Pizarro JC, Seitova A, Trimble WS, Saftig P, Grinstein S, Dhe-Paganon S., Nature 504(7478), 2013
PMID: 24162852
Scavenger receptor B2 is a cellular receptor for enterovirus 71.
Yamayoshi S, Yamashita Y, Li J, Hanagata N, Minowa T, Takemura T, Koike S., Nat. Med. 15(7), 2009
PMID: 19543282
Human SCARB2-dependent infection by coxsackievirus A7, A14, and A16 and enterovirus 71
Yamayoshi, J. Virol. 86(), 2012
A role for the lysosomal membrane protein LGP85 in the biogenesis and maintenance of endosomal and lysosomal morphology
Kuronita, J. Cell. Sci. 115(), 2002
Array-based gene discovery with three unrelated subjects shows SCARB2/LIMP-2 deficiency causes myoclonus epilepsy and glomerulosclerosis.
Berkovic SF, Dibbens LM, Oshlack A, Silver JD, Katerelos M, Vears DF, Lullmann-Rauch R, Blanz J, Zhang KW, Stankovich J, Kalnins RM, Dowling JP, Andermann E, Andermann F, Faldini E, D'Hooge R, Vadlamudi L, Macdonell RA, Hodgson BL, Bayly MA, Savige J, Mulley JC, Smyth GK, Power DA, Saftig P, Bahlo M., Am. J. Hum. Genet. 82(3), 2008
PMID: 18308289
SCARB2 mutations in progressive myoclonus epilepsy (PME) without renal failure.
Dibbens LM, Michelucci R, Gambardella A, Andermann F, Rubboli G, Bayly MA, Joensuu T, Vears DF, Franceschetti S, Canafoglia L, Wallace R, Bassuk AG, Power DA, Tassinari CA, Andermann E, Lehesjoki AE, Berkovic SF., Ann. Neurol. 66(4), 2009
PMID: 19847901
Proteolytic cleavage of the disease-related lysosomal membrane glycoprotein CLN7.
Steenhuis P, Froemming J, Reinheckel T, Storch S., Biochim. Biophys. Acta 1822(10), 2012
PMID: 22668694
Disrupted in renal carcinoma 2 (DIRC2), a novel transporter of the lysosomal membrane, is proteolytically processed by cathepsin L.
Savalas LR, Gasnier B, Damme M, Lubke T, Wrocklage C, Debacker C, Jezegou A, Reinheckel T, Hasilik A, Saftig P, Schroder B., Biochem. J. 439(1), 2011
PMID: 21692750
Analysis of the biogenesis of heparan sulfate acetyl-CoA:alpha-glucosaminide N-acetyltransferase provides insights into the mechanism underlying its complete deficiency in mucopolysaccharidosis IIIC
Durand, J. Biol. Chem. 285(), 2010
Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain
Santamaria, J. Biol. Chem. 274(), 1999
Human cathepsin F. Molecular cloning, functional expression, tissue localization, and enzymatic characterization
Wang, J. Biol. Chem. 273(), 1998
Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
Shi, J. Exp. Med. 191(), 2000
Cysteine protease cathepsin F is expressed in human atherosclerotic lesions, is secreted by cultured macrophages, and modifies low density lipoprotein particles in vitro
Oorni, J. Biol. Chem. 279(), 2004
Cathepsin F mutations cause Type B Kufs disease, an adult-onset neuronal ceroid lipofuscinosis.
Smith KR, Dahl HH, Canafoglia L, Andermann E, Damiano J, Morbin M, Bruni AC, Giaccone G, Cossette P, Saftig P, Grotzinger J, Schwake M, Andermann F, Staropoli JF, Sims KB, Mole SE, Franceschetti S, Alexander NA, Cooper JD, Chapman HA, Carpenter S, Berkovic SF, Bahlo M., Hum. Mol. Genet. 22(7), 2013
PMID: 23297359
Pseudo-dominant inheritance of a novel CTSF mutation associated with type B Kufs disease.
Di Fabio R, Moro F, Pestillo L, Meschini MC, Pezzini F, Doccini S, Casali C, Pierelli F, Simonati A, Santorelli FM., Neurology 83(19), 2014
PMID: 25274848
Neuronal ceroid lipofuscinoses.
Jalanko A, Braulke T., Biochim. Biophys. Acta 1793(4), 2008
PMID: 19084560
LIMP-2/LGP85 deficiency causes ureteric pelvic junction obstruction, deafness and peripheral neuropathy in mice.
Gamp AC, Tanaka Y, Lullmann-Rauch R, Wittke D, D'Hooge R, De Deyn PP, Moser T, Maier H, Hartmann D, Reiss K, Illert AL, von Figura K, Saftig P., Hum. Mol. Genet. 12(6), 2003
PMID: 12620969
NCU-G1 is a highly glycosylated integral membrane protein of the lysosome.
Schieweck O, Damme M, Schroder B, Hasilik A, Schmidt B, Lubke T., Biochem. J. 422(1), 2009
PMID: 19489740
LIMP-2 expression is critical for β-glucocerebrosidase activity and α-synuclein clearance.
Rothaug M, Zunke F, Mazzulli JR, Schweizer M, Altmeppen H, Lullmann-Rauch R, Kallemeijn WW, Gaspar P, Aerts JM, Glatzel M, Saftig P, Krainc D, Schwake M, Blanz J., Proc. Natl. Acad. Sci. U.S.A. 111(43), 2014
PMID: 25316793
Human cathepsins F and W: A new subgroup of cathepsins.
Wex T, Levy B, Wex H, Bromme D., Biochem. Biophys. Res. Commun. 259(2), 1999
PMID: 10362521
Bafilomycin A1, a specific inhibitor of vacuolar-type H(+)-ATPase, inhibits acidification and protein degradation in lysosomes of cultured cells
Yoshimori, J. Biol. Chem. 266(), 1991
On the effects of weak bases and monensin on sorting and processing of lysosomal enzymes in human cells.
Braulke T, Geuze HJ, Slot JW, Hasilik A, von Figura K., Eur. J. Cell Biol. 43(3), 1987
PMID: 3040410
Biosynthesis, glycosylation, movement through the Golgi system, and transport to lysosomes by an N-linked carbohydrate-independent mechanism of three lysosomal integral membrane proteins
Barriocanal, J. Biol. Chem. 261(), 1986
Normal lysosomal morphology and function in LAMP-1-deficient mice
Andrejewski, J. Biol. Chem. 274(), 1999
Molecular mechanism of SCARB2-mediated attachment and uncoating of EV71.
Dang M, Wang X, Wang Q, Wang Y, Lin J, Sun Y, Li X, Zhang L, Lou Z, Wang J, Rao Z., Protein Cell 5(9), 2014
PMID: 24986489
Lysosome sorting of β-glucocerebrosidase by LIMP-2 is targeted by the mannose 6-phosphate receptor.
Zhao Y, Ren J, Padilla-Parra S, Fry EE, Stuart DI., Nat Commun 5(), 2014
PMID: 25027712
Kufs' disease: a critical reappraisal.
Berkovic SF, Carpenter S, Andermann F, Andermann E, Wolfe LS., Brain 111 ( Pt 1)(), 1988
PMID: 3284607
Kufs disease, the major adult form of neuronal ceroid lipofuscinosis, caused by mutations in CLN6.
Arsov T, Smith KR, Damiano J, Franceschetti S, Canafoglia L, Bromhead CJ, Andermann E, Vears DF, Cossette P, Rajagopalan S, McDougall A, Sofia V, Farrell M, Aguglia U, Zini A, Meletti S, Morbin M, Mullen S, Andermann F, Mole SE, Bahlo M, Berkovic SF., Am. J. Hum. Genet. 88(5), 2011
PMID: 21549341
Murine cathepsin F deficiency causes neuronal lipofuscinosis and late-onset neurological disease.
Tang CH, Lee JW, Galvez MG, Robillard L, Mole SE, Chapman HA., Mol. Cell. Biol. 26(6), 2006
PMID: 16508006
Cathepsin D deficiency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons
Koike, J. Neurosci. 20(), 2000
Neuronal loss and brain atrophy in mice lacking cathepsins B and L.
Felbor U, Kessler B, Mothes W, Goebel HH, Ploegh HL, Bronson RT, Olsen BR., Proc. Natl. Acad. Sci. U.S.A. 99(12), 2002
PMID: 12048238
Autophagy in lysosomal storage disorders.
Lieberman AP, Puertollano R, Raben N, Slaugenhaupt S, Walkley SU, Ballabio A., Autophagy 8(5), 2012
PMID: 22647656

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