Structural highlightsFunctionLAMP1_HUMAN Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, autophagy, and cholesterol homeostasis (By similarity). Also plays an important role in NK-cells cytotoxicity (PubMed:23632890, PubMed:2022921). Mechanistically, participates in cytotoxic granule movement to the cell surface and perforin trafficking to the lytic granule (PubMed:23632890). In addition, protects NK-cells from degranulation-associated damage induced by their own cytotoxic granule content (PubMed:23847195). Presents carbohydrate ligands to selectins. Also implicated in tumor cell metastasis.[UniProtKB:P11438][1] [2] [3] (Microbial infection) Acts as a receptor for Lassa virus glycoprotein (PubMed:24970085, PubMed:25972533, PubMed:27605678, PubMed:28448640). Promotes also fusion of the virus with host membrane in less acidic endosomes (PubMed:29295909).[4] [5] [6] [7] [8] (Microbial infection) Supports the FURIN-mediated cleavage of mumps virus fusion protein F by interacting with both FURIN and the unprocessed form but not the processed form of the viral protein F.[9]
References
- ↑ Peters PJ, Borst J, Oorschot V, Fukuda M, Krähenbühl O, Tschopp J, Slot JW, Geuze HJ. Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes. J Exp Med. 1991 May 1;173(5):1099-109. PMID:2022921 doi:10.1084/jem.173.5.1099
- ↑ Krzewski K, Gil-Krzewska A, Nguyen V, Peruzzi G, Coligan JE. LAMP1/CD107a is required for efficient perforin delivery to lytic granules and NK-cell cytotoxicity. Blood. 2013 Jun 6;121(23):4672-83. PMID:23632890 doi:10.1182/blood-2012-08-453738
- ↑ Cohnen A, Chiang SC, Stojanovic A, Schmidt H, Claus M, Saftig P, Janßen O, Cerwenka A, Bryceson YT, Watzl C. Surface CD107a/LAMP-1 protects natural killer cells from degranulation-associated damage. Blood. 2013 Aug 22;122(8):1411-8. PMID:23847195 doi:10.1182/blood-2012-07-441832
- ↑ Jae LT, Raaben M, Herbert AS, Kuehne AI, Wirchnianski AS, Soh TK, Stubbs SH, Janssen H, Damme M, Saftig P, Whelan SP, Dye JM, Brummelkamp TR. Virus entry. Lassa virus entry requires a trigger-induced receptor switch. Science. 2014 Jun 27;344(6191):1506-10. doi: 10.1126/science.1252480. PMID:24970085 doi:http://dx.doi.org/10.1126/science.1252480
- ↑ Cohen-Dvashi H, Cohen N, Israeli H, Diskin R. Molecular mechanism for LAMP1 recognition by Lassa Virus. J Virol. 2015 May 13. pii: JVI.00651-15. PMID:25972533 doi:http://dx.doi.org/10.1128/JVI.00651-15
- ↑ Cohen-Dvashi H, Israeli H, Shani O, Katz A, Diskin R. Role of LAMP1 Binding and pH Sensing by the Spike Complex of Lassa Virus. J Virol. 2016 Oct 28;90(22):10329-10338. Print 2016 Nov 15. PMID:27605678 doi:http://dx.doi.org/10.1128/JVI.01624-16
- ↑ Israeli H, Cohen-Dvashi H, Shulman A, Shimon A, Diskin R. Mapping of the Lassa virus LAMP1 binding site reveals unique determinants not shared by other old world arenaviruses. PLoS Pathog. 2017 Apr 27;13(4):e1006337. doi: 10.1371/journal.ppat.1006337., eCollection 2017 Apr. PMID:28448640 doi:http://dx.doi.org/10.1371/journal.ppat.1006337
- ↑ Hulseberg CE, Fénéant L, Szymańska KM, White JM. Lamp1 Increases the Efficiency of Lassa Virus Infection by Promoting Fusion in Less Acidic Endosomal Compartments. mBio. 2018 Jan 2;9(1):e01818-17. PMID:29295909 doi:10.1128/mBio.01818-17
- ↑ Ueo A, Kubota M, Shirogane Y, Ohno S, Hashiguchi T, Yanagi Y. Lysosome-Associated Membrane Proteins Support the Furin-Mediated Processing of the Mumps Virus Fusion Protein. J Virol. 2020 Jun 1;94(12):e00050-20. PMID:32295904 doi:10.1128/JVI.00050-20
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