Biology:PLDN
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Generic protein structure example |
Pallidin is a protein that in humans is encoded by the PLDN gene.[1][2]
Function
The protein encoded by this gene may play a role in intracellular vesicle trafficking. It interacts with Syntaxin 13 which mediates intracellular membrane fusion. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.[2]
Interactions
PLDN has been shown to interact with:
References
- ↑ 1.0 1.1 "The pallid gene encodes a novel, syntaxin 13-interacting protein involved in platelet storage pool deficiency". Nat Genet 23 (3): 329–32. Dec 1999. doi:10.1038/15507. PMID 10610180.
- ↑ 2.0 2.1 "Entrez Gene: PLDN pallidin homolog (mouse)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=26258.
- ↑ 3.0 3.1 3.2 3.3 3.4 3.5 "Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1)". J. Biol. Chem. 279 (27): 28393–401. Jul 2004. doi:10.1074/jbc.M402513200. PMID 15102850.
- ↑ "BLOC-1, a novel complex containing the pallidin and muted proteins involved in the biogenesis of melanosomes and platelet-dense granules". J. Biol. Chem. 277 (31): 28191–9. Aug 2002. doi:10.1074/jbc.M204011200. PMID 12019270.
Further reading
- "The pallidin (Pldn) gene and the role of SNARE proteins in melanosome biogenesis". Pigment Cell Res. 15 (2): 82–6. 2002. doi:10.1034/j.1600-0749.2002.1r082.x. PMID 11936273.
- "Associations of human erythrocyte band 4.2. Binding to ankyrin and to the cytoplasmic domain of band 3". J. Biol. Chem. 263 (21): 10212–8. 1988. doi:10.1016/S0021-9258(19)81500-4. PMID 2968981.
- "Human erythrocyte dematin and protein 4.2 (pallidin) are ATP binding proteins". Biochemistry 35 (9): 3001–6. 1996. doi:10.1021/bi951745y. PMID 8608138.
- "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. 1996. doi:10.1006/abio.1996.0138. PMID 8619474.
- "Role of N-myristylation in targeting of band 4.2 (pallidin) in nonerythroid cells". Exp. Cell Res. 229 (2): 421–31. 1997. doi:10.1006/excr.1996.0387. PMID 8986625.
- "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. 1997. doi:10.1101/gr.7.4.353. PMID 9110174.
- "BLOC-1, a novel complex containing the pallidin and muted proteins involved in the biogenesis of melanosomes and platelet-dense granules". J. Biol. Chem. 277 (31): 28191–9. 2002. doi:10.1074/jbc.M204011200. PMID 12019270.
- "Pallidin is a component of a multi-protein complex involved in the biogenesis of lysosome-related organelles". Traffic 3 (9): 666–77. 2003. doi:10.1034/j.1600-0854.2002.30908.x. PMID 12191018.
- "Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel protein that is part of the pallidin-muted complex (BLOC-1)". Blood 101 (11): 4402–7. 2003. doi:10.1182/blood-2003-01-0020. PMID 12576321. http://www.bloodjournal.org/cgi/content/abstract/101/11/4402.
- "Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1)". Nat. Genet. 35 (1): 84–9. 2003. doi:10.1038/ng1229. PMID 12923531.
- "Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1)". J. Biol. Chem. 279 (27): 28393–401. 2004. doi:10.1074/jbc.M402513200. PMID 15102850.
- "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. 2005. doi:10.1016/j.cell.2005.08.029. PMID 16169070.