Abstract
AbstractLysosomes are the site of degradation of obsolete intracellular material during autophagy and of extracellular macromolecules following endocytosis and phagocytosis. The membrane of lysosomes and late endosomes is enriched in highly glycosylated transmembrane proteins of largely unknown function. Significant progress has been made in recent years towards elucidating the pathways by which these lysosomal membrane proteins are delivered to late endosomes and lysosomes. While some lysosomal membrane proteins follow the constitutive secretory pathway and reach lysosomes indirectly via the cell surface and endocytosis, others exit the trans‐Golgi network in clathrin‐coated vesicles for direct delivery to endosomes and lysosomes. Sorting from the Golgi or the plasma membrane into the endosomal system is mediated by signals encoded by the short cytosolic domain of these proteins. This review will discuss the role of lysosomal membrane proteins in the biogenesis of the late endosomal and lysosomal membranes, with particular emphasis on the structural features and molecular mechanisms underlying the intracellular trafficking of these proteins.
References
88
Referenced
207
10.1111/j.1432-1033.1983.tb07841.x
10.1146/annurev.cb.05.110189.002411
10.1083/jcb.107.6.2491
10.1016/S0092-8674(88)80026-6
10.4049/jimmunol.151.8.3988
/ J. Immunol. / Immunogenic peptides bind to Class‐II MHC molecules in an early lysosomal compartment by Harding C. V. (1993)10.1084/jem.173.5.1099
10.1083/jcb.100.6.1839
10.1083/jcb.99.4.1511
10.1016/S0021-9258(18)37369-1
/ J. Biol. Chem. / Isolation and characterization of human lysosomal membrane glycoproteins, h‐iamp‐1 and h‐lamp‐2 by Carlsson S. R. (1988)10.1083/jcb.101.1.85
10.1016/0092-8674(87)90543-5
10.1016/S0021-9258(18)37370-8
/ J. Biol. Chem. / Cloning of cDNAs encoding human lysosomal membrane glycoproteins, h‐lamp‐1 and h‐lamp‐2 by Fukuda M. (1988)10.1073/pnas.85.11.3743
10.1016/S0021-9258(19)34076-1
/ J. Biol. Chem. / The cDNA sequence of mouse lamp‐2 by Cha Y. (1990){'key': 'e_1_2_1_16_2', 'first-page': '8745', 'article-title': 'Isolation and sequencing of a cDNA clone encoding lysosomal membrane glycoprotein mouse lamp‐1', 'volume': '263', 'author': 'Chen J. W.', 'year': '1988', 'journal-title': 'J. Biol. Chem.'}
/ J. Biol. Chem. / Isolation and sequencing of a cDNA clone encoding lysosomal membrane glycoprotein mouse lamp‐1 by Chen J. W. (1988)10.1016/S0021-9258(19)38504-7
/ J. Biol. Chem. / Characterization and cloning of lgp110, a lysosoma membrane glycoprotein from mouse and rat cells by Granger B. L. (1990)10.1016/0014-5793(89)80561-7
10.1073/pnas.85.20.7577
10.1083/jcb.106.1.61
10.1242/jcs.108.5.2093
/ J. Cell Sci. / Multiple mRNAs encode the avian lysosomal membrane protein LAMP‐2, resulting in alternative transmembrane and cytoplasmic domains by Hatem C. L. (1995)10.1016/S0021-9258(19)47094-4
/ J. Biol. Chem. / Structure of human lysosomal membrane glycoprotein 1: assignment of disulfide bonds and visualization of its domain arrangement by Carlsson S. R. (1989)10.1016/S0021-9258(19)39130-6
/ J. Biol. Chem. / The disulfide structure of mouse lysosomes‐associated membrane protein 1 by Arterburn L. M. (1990)10.1089/dna.1995.14.863
10.1016/S0021-9258(19)39148-3
/ J. Biol. Chem. / Two human lysosome membrane glycoproteins, h‐lamp‐1 and h‐lamp‐2, are encoded by genes localized to chromosome 13q34 and chromosome Xq24–25, respectively by Mattei M.‐G. (1990)10.1016/S0021-9258(18)52972-0
/ J. Biol. Chem. / The genes of major lysosomal membrane glycoproteins, lamp‐1 and lamp‐2: the 5' flanking sequence of lamp‐2 gene and comparison of exon organization in two genes by Sawada R. (1993)10.1016/S0021-9258(17)45315-4
/ J. Biol. Chem. / Structure of a gene for a lysosomal membrane glycoprotein (LEP100). Housekeeping gene with unexpected exon organization by Zot A. S. (1990)10.1016/S0021-9258(18)49980-2
10.1016/0167-4781(94)90291-7
10.4049/jimmunol.149.3.862
/ J. Immunol. / The rat mast cell antigen AD1 (homologue to human CD63 or melanoma antigen ME491) is expressed in other cells in culture by Nishikata H. (1992)10.1016/0006-291X(91)90127-S
10.1016/S0021-9258(18)55375-8
/ J. Biol. Chem. / Cloning, sequencing and expression of a cDNA encoding rat limp II, a novel 74 kDa lysosomal membrane protein related to the surface adhesion protein CD36 by Vega M. A. (1991)10.1002/j.1460-2075.1988.tb03078.x
10.1016/0006-291X(89)90779-1
10.1002/j.1460-2075.1988.tb03079.x
10.1083/jcb.105.3.1227
10.1016/S0021-9258(18)66630-X
/ J. Biol. Chem. / Biosynthesis, glycosylation, movement through the golgi system and transport to lysosomes by an N‐linked carbohydrate‐independent mechanism of three lysosomal integral membrane proteins by Barrioccanal J. G. (1986)10.1016/S0021-9258(17)44784-3
10.1182/blood.V80.6.1470.1470
10.1083/jcb.108.4.1291
10.1083/jcb.118.5.1027
10.1093/oxfordjournals.jbchem.a122921
/ J. Biochem. / Morphological localization of a major lysosomal membrane glycoprotin in the endocytic membrane system by Furuno K. (1989)10.1093/oxfordjournals.jbchem.a122922
/ J. Biochem. / Biochemical analysis of the movement of a major lysosomal membrane glycoprotein in the endocytic membrane system by Furuno K. (1989)10.1016/0003-9861(89)90597-3
10.1016/0006-291X(90)90990-5
10.1083/jcb.115.6.1573
10.1002/j.1460-2075.1989.tb08537.x
10.1016/0006-291X(90)90501-D
10.1016/S0021-9258(18)31422-4
10.1016/0003-9861(85)90727-1
10.1083/jcb.100.6.1839
10.1083/jcb.117.2.311
10.1083/jcb.128.3.321
10.1016/0003-9861(86)90030-5
10.1083/jcb.111.3.955
10.1016/0003-9861(92)90619-8
10.1126/science.7569928
10.1016/S0021-9258(18)55288-1
/ J. Biol. Chem. / Targeting of lysosomal integral membrane protein LIMP II. The tyrosine‐lacking carboxyl cytoplasmic tail of LIMP II is sufficient for direct targeting to lysosomes by Vega M. A. (1991)10.1016/S0021-9258(17)37676-7
/ J. Biol. Chem. / Lysosomal targeting of limp II membrane glycoprotein requires a novel Leu‐Ile motif at a particular position in its cytoplasmic tail by Ogata S. (1994)10.1016/S0021-9258(17)37418-5
/ J. Biol. Chem. / The residues Leu(Ile)(475)‐Ile(Leu, Val, Aal)(476), contained in the extended carboxyl cytoplasmic tail, are critical for targeting of the resident lysosomal membrane protein limp II to lysosomes by Sandoval I. V. (1994)10.1016/S0021-9258(18)41900-X
10.1002/j.1460-2075.1994.tb06594.x
10.1016/0092-8674(92)90636-Q
10.1007/978-1-4615-2401-4_7
10.1042/bj2590569
10.1016/S0021-9258(18)42823-2
10.1016/S0021-9258(18)31441-8
10.1016/S0021-9258(17)42275-7
10.1016/S0021-9258(18)53945-4
/ J. Biol. Chem. / The motif Tyr‐X‐X‐hydrophobic residue mediates lysosomal membrane targeting of lysosome‐associated membrane protein‐1 by Guarnieri F. G. (1993)10.1016/0092-8674(91)90437-4
10.1002/j.1460-2075.1990.tb07558.x
{'key': 'e_1_2_1_72_2', 'first-page': '16269', 'article-title': 'Targeting of ysosomal integral membrane protein LIMP II', 'volume': '266', 'author': 'Vega M. A.', 'year': '1991', 'journal-title': 'J. Biol. Chem.'}
/ J. Biol. Chem. / Targeting of ysosomal integral membrane protein LIMP II by Vega M. A. (1991)10.1002/j.1460-2075.1992.tb05539.x
10.1016/0092-8674(91)90296-B
10.1002/j.1460-2075.1993.tb05866.x
-
Rodriguez‐Boulan E.andZurzolo C.(1993). Polarity signals in epithelial cells.J. Cell Sci.Suppl. 9–12.
(
10.1242/jcs.1993.Supplement_17.2
) 10.1016/0955-0674(94)90073-6
10.1016/0955-0674(94)90074-4
10.1146/annurev.cb.11.110195.001411
{'key': 'e_1_2_1_80_2', 'first-page': '3', 'article-title': 'A novel lysosomal compartment engaged in antigen presentation', 'volume': '64', 'author': 'Geuze H.', 'year': '1994', 'journal-title': 'Eur. J. Cell Biol.'}
/ Eur. J. Cell Biol. / A novel lysosomal compartment engaged in antigen presentation by Geuze H. (1994)10.1038/349669a0
10.1016/0092-8674(90)90137-4
10.1083/jcb.126.2.317
10.1083/jcb.131.2.351
10.1084/jem.182.2.325
10.1038/369103a0
-
Raposo G.et al.(1996). B‐lymphocytes secrete antigen presenting vesicles.J. Exp. Med. (in press).
(
10.1084/jem.183.3.1161
) 10.1083/jcb.124.4.435
10.1083/jcb.130.6.1297
Dates
Type | When |
---|---|
Created | 20 years, 5 months ago (Feb. 25, 2005, 3:15 a.m.) |
Deposited | 1 year, 9 months ago (Oct. 27, 2023, 9:36 a.m.) |
Indexed | 1 month, 4 weeks ago (June 23, 2025, 2:45 a.m.) |
Issued | 29 years, 3 months ago (May 1, 1996) |
Published | 29 years, 3 months ago (May 1, 1996) |
Published Online | 20 years, 6 months ago (Feb. 5, 2005) |
Published Print | 29 years, 3 months ago (May 1, 1996) |
@article{Hunziker_1996, title={Intracellular trafficking of lysosomal membrane proteins}, volume={18}, ISSN={1521-1878}, url={http://dx.doi.org/10.1002/bies.950180508}, DOI={10.1002/bies.950180508}, number={5}, journal={BioEssays}, publisher={Wiley}, author={Hunziker, Walter and Geuze, Hans J.}, year={1996}, month=may, pages={379–389} }