Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15

Molecular Biology of the Cell

Volumn 24, Issue 16, 2013, Pages 2558-2569

  Hirst, Jennifer ^a   Borner, Georg H H ^a   Edgar, James ^a   Hein, Marco Y ^b   Mann, Matthias ^b   Buchholz, Frank ^c   Antrobus, Robin ^a   Robinson, Margaret S ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^c DRESDEN UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 5 PHOSPHONOVALERIC ACID; CLATHRIN HEAVY CHAIN; COAT PROTEIN COMPLEX I; PROTEIN; SOMATOMEDIN B RECEPTOR; SPG11 PROTEIN; SPG15 PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; CYTOSOL; ENDOSOME; GENE CLUSTER; GENE MUTATION; GENE SILENCING; GENETIC ASSOCIATION; HEREDITARY MOTOR SENSORY NEUROPATHY; HUMAN; HUMAN CELL; HUMAN TISSUE; IN VITRO STUDY; LYSOSOME; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN TARGETING; STOICHIOMETRY;

CARRIER PROTEINS; CELL LINE, TUMOR; ENDOSOMES; HELA CELLS; HUMANS; MULTIPROTEIN COMPLEXES; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; PROTEINS; RECEPTOR, IGF TYPE 2; RNA INTERFERENCE; RNA, SMALL INTERFERING; SPASTIC PARAPLEGIA, HEREDITARY; TRANS-ACTIVATORS;

EID: 84882739113     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E13-03-0170     Document Type: Article

References (39)

1. Antrobus R, Borner GHH (2011). Improved elution conditions for native co-immunoprecipitation. PLoS One 23, e18218.
2. Arike L, Valgepea K, Peil L, Nahku R, Adamberg K, Vilu R (2012). Comparison and applications of label-free absolute proteome quantification methods on Escherichia coli. J Proteomics 75, 5437-5448.
3. Beck KA, Keen JH (1991). Interaction of phosphoinositide cycle intermediates with the plasma membrane-associated clathrin assembly protein AP-2. J Biol Chem 266, 4442-4447.
4. Bettencourt C et al. (2013). Exome sequencing is a useful diagnostic tool for complicated forms of hereditary spastic paraplegia. Clin Genet, doi: 10.1111/cge.12133.
5. Boukhris A et al. (2008). Hereditary spastic paraplegia with mental impairment and thin corpus callosum in Tunisia: SPG11, SPG15, and further genetic heterogeneity. Arch Neurol 65, 393-402.
6. Brankatschk B, Pons V, Parton RG, Gruenberg J (2011). Role of SNX16 in the dynamics of tubulo-cisternal membrane domains of late endosomes. PLoS One 6, e21771.
7. Cai Q, Lu L, Tian JH, Zhu YB, Qiao H, Sheng ZH (2010). Snapin-regulated late endosomal transport is critical for efficient autophagy-lysosomal function in neurons. Neuron 68, 73-86.
8. Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ (2002). Molecular architecture and functional model of the endocytic AP2 complex. Cell 109, 523-535.
9. Cox J, Mann M (2008). MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26, 1367-1372.
10. Devos D, Dokudovskaya S, Alber F, Williams R, Chait BT, Sali A, Rout MP (2004). Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PLoS Biol 2, e380.
11. Finsterer J, Löscher W, Quasthoff S, Wanschitz J, Auer-Grumbach M, Stevanin G (2012). Hereditary spastic paraplegias with autosomal dominant, recessive, X-linked, or maternal trait of inheritance. J Neurol Sci 318, 1-18.
12. Gonzalez MA, Lebrigio RF, Van Booven D, Ulloa RH, Powell E, Speziani F, Tekin M, Schüle R, Züchner S (2013). GEnomes Management Application (GEM.app): a new software tool for large-scale collaborative genome analysis. Hum Mutat 34, 842-846.
13. Hanein S et al. (2008). Identification of the SPG15 gene, encoding spastizin, as a frequent cause of complicated autosomal-recessive spastic paraplegia, including Kjellin syndrome. Am J Hum Genet 82, 992-1002.
14. Hanson BJ, Hong W (2003). Evidence for a role of SNX16 in regulating traffic between the early and later endosomal compartments. J Biol Chem 278, 34617-34630.
15. Harbour ME, Breusegem SY, Antrobus R, Freeman C, Reid E, Seaman MNJ (2010). The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics. J Cell Sci 123, 3703-3717.
16. Haucke V (2005). Phosphoinositide regulation of clathrin-mediated endocytosis. Biochem Soc Trans 33, 1285-1289.
17. Hirst J, Barlow LD, Francisco GC, Sahlender DA, Seaman MNJ, Dacks JB, Robinson MS (2011). The fifth adaptor protein complex. PLoS Biol 9, e1001170.
18. Hirst J, Borner GHH, Antrobus R, Peden AA, Hodson NA, Sahlender DA, Robinson MS (2012). Distinct and overlapping roles for AP-1 and GGAs revealed by the "knocksideways" system. Curr Biol 22, 1711-1716.
19. Hirst J, Irving C, Borner GHH (2013). Adaptor protein complexes AP-4 and AP-5: new players in endosomal trafficking and progressive spastic paraplegia. Traffic 14, 153-164.
20. Hirst J, Sahlender DA, Choma M, Sinka R, Harbour ME, Parkinson M, Robinson MS (2009). Spatial and functional relationship of GGAs and AP-1 in Drosophila and HeLa cells. Traffic 10, 1696-1710.
21. Honing S, Ricotta D, Krauss M, Spate K, Spolaore B, Motley A, Robinson M, Robinson C, Haucke V, Owen DJ (2005). Phosphatidylinositol-(4,5)-bisphosphate regulates sorting signal recognition by the clathrin-associated adaptor complex AP2. Mol Cell 18, 519-531.
22. Hubner NC, Bird AW, Cox J, Splettstoesser B, Bandilla P, Poser I, Hyman A, Mann M (2010). Quantitative proteomics combined with BAC TransgeneOmics reveals in vivo protein interactions. J Cell Biol 189, 739-754.
23. Hubner NC, Mann M (2011). Extracting gene function from protein-protein interactions using Quantitative BAC InteraCtomics (QUBIC). Methods 53, 453-459.
24. Lemmon SK, Traub LM (2012). Getting in touch with the clathrin terminal domain. Traffic 13, 511-519.
25. Martin E, Yanicostas C, Rastetter A, Naini SM, Maouedj A, Kabashi E, Rivaud-Péchoux S, Brice A, Stevanin G, Soussi-Yanicostas N (2012). Spatacsin and spastizin act in the same pathway required for proper spinal motor neuron axon outgrowth in zebrafish. Neurobiol Dis 48, 299-308.
26. McGuffin LJ, Bryson K, Jones DT (2000). The PSIPRED protein structure prediction server. Bioinformatics 16, 404-405.
27. Murmu RP et al. (2011). Cellular distribution and subcellular localization of spatacsin and spastizin, two proteins involved in hereditary spastic paraplegia. Mol Cell Neurosci 47, 191-202.
28. Page LJ, Robinson MS (1995). Targeting signals and subunit interactions in coated vesicle adaptor complexes. J Cell Biol 131, 619-630.
29. Pavel J, Harter C, Wieland FT (1998). Reversible dissociation of coatomer: functional characterization of a beta/delta-coat protein subcomplex. Proc Natl Acad Sci USA 95, 2140-2145.
30. Raiborg C, Bache KG, Gillooly DJ, Madshus IH, Stang E, Stenmark H (2002). Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of early endosomes. Nat Cell Biol 4, 394-398.
31. Sagona AP, Nezis IP, Pedersen NM, Liestøl K, Poulton J, Rusten TE, Skotheim RI, Raiborg C, Stenmark H (2010). PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody. Nat Cell Biol 12, 362-371.
32. Schwanhäusser B, Busse D, Li N, Dittmar G, Schuchhardt J, Wolf J, Chen W, Selbach M (2011). Global quantification of mammalian gene expression control. Nature 473, 337-342.
33. Simpson F, Bright NA, West MA, Newman LS, Darnell RB, Robinson MS (1996). A novel adaptor-related protein complex. J Cell Biol 133, 749-760.
34. Slabicki M et al. (2010). A genome-scale DNA repair RNAi screen identifies SPG48 as a novel gene associated with hereditary spastic paraplegia. PLoS Biol 8, e1000408.
35. Söding J, Biegert A, Lupas AN (2005). The HHpred interactive server for protein homology detection and structure prediction. Nucleic Acids Res 33, W244-W248.
36. Tiwari RK, Kusari J, Sen GC (1987). Functional equivalents of interferon-mediated signals needed for induction of an mRNA can be generated by double-stranded RNA and growth factors. EMBO J 6, 3373-3378.
37. Tsukita S, Ishikawa H (1980). The movement of membranous organelles in axons. Electron microscopic identification of anterogradely and retrogradely transported organelles. J Cell Biol 84, 513-530.
38. Wisniewski JR, Zougman A, Nagaraj N, Mann M (2009). Universal sample preparation method for proteome analysis. Nat Methods 6, 359-362.
39. Züchner S (2010). Peripheral neuropathies: whole genome sequencing identifies causal variants in CMT. Nat Rev Neurosci 6, 424-425.