trans-Golgi Network Vesicle Budding (Homo sapiens)

From WikiPathways

Description

Quality Tags

Ontology Terms

Saving...

Bibliography

1. Sohda M, Misumi Y, Yamamoto A, Yano A, Nakamura N, Ikehara Y.; ''Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin.''; PubMed Europe PMC Scholia
2. Suzuki K, Verma IM.; ''Phosphorylation of SNAP-23 by IkappaB kinase 2 regulates mast cell degranulation.''; PubMed Europe PMC Scholia
3. Puri N, Roche PA.; ''Ternary SNARE complexes are enriched in lipid rafts during mast cell exocytosis.''; PubMed Europe PMC Scholia
4. Hirst J, Bright NA, Rous B, Robinson MS.; ''Characterization of a fourth adaptor-related protein complex.''; PubMed Europe PMC Scholia
5. Zhu Y, Traub LM, Kornfeld S.; ''ADP-ribosylation factor 1 transiently activates high-affinity adaptor protein complex AP-1 binding sites on Golgi membranes.''; PubMed Europe PMC Scholia
6. Ungewickell E, Ungewickell H, Holstein SE, Lindner R, Prasad K, Barouch W, Martin B, Greene LE, Eisenberg E.; ''Role of auxilin in uncoating clathrin-coated vesicles.''; PubMed Europe PMC Scholia
7. Musacchio A, Smith CJ, Roseman AM, Harrison SC, Kirchhausen T, Pearse BM.; ''Functional organization of clathrin in coats: combining electron cryomicroscopy and X-ray crystallography.''; PubMed Europe PMC Scholia
8. Takatsu H, Sakurai M, Shin HW, Murakami K, Nakayama K.; ''Identification and characterization of novel clathrin adaptor-related proteins.''; PubMed Europe PMC Scholia
9. Bryant NJ, Govers R, James DE.; ''Regulated transport of the glucose transporter GLUT4.''; PubMed Europe PMC Scholia
10. Antonin W, Holroyd C, Fasshauer D, Pabst S, Von Mollard GF, Jahn R.; ''A SNARE complex mediating fusion of late endosomes defines conserved properties of SNARE structure and function.''; PubMed Europe PMC Scholia
11. Starcevic M, Dell'Angelica EC.; ''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).''; PubMed Europe PMC Scholia
12. Wesolowski J, Paumet F.; ''Escherichia coli exposure inhibits exocytic SNARE-mediated membrane fusion in mast cells.''; PubMed Europe PMC Scholia
13. Lee DW, Zhao X, Zhang F, Eisenberg E, Greene LE.; ''Depletion of GAK/auxilin 2 inhibits receptor-mediated endocytosis and recruitment of both clathrin and clathrin adaptors.''; PubMed Europe PMC Scholia
14. Hartmann-Stühler C, Prange R.; ''Hepatitis B virus large envelope protein interacts with gamma2-adaptin, a clathrin adaptor-related protein.''; PubMed Europe PMC Scholia
15. Acton SL, Wong DH, Parham P, Brodsky FM, Jackson AP.; ''Alteration of clathrin light chain expression by transfection and gene disruption.''; PubMed Europe PMC Scholia
16. Salinas E, Quintanar-Stephano A, Córdova LE, Ouintanar JL.; ''Allergen-sensitization increases mast-cell expression of the exocytotic proteins SNAP-23 and syntaxin 4, which are involved in histamine secretion.''; PubMed Europe PMC Scholia
17. Rost M, Mann S, Lambert C, Döring T, Thomé N, Prange R.; ''Gamma-adaptin, a novel ubiquitin-interacting adaptor, and Nedd4 ubiquitin ligase control hepatitis B virus maturation.''; PubMed Europe PMC Scholia
18. Katoh Y, Ritter B, Gaffry T, Blondeau F, Höning S, McPherson PS.; ''The clavesin family, neuron-specific lipid- and clathrin-binding Sec14 proteins regulating lysosomal morphology.''; PubMed Europe PMC Scholia
19. Döring T, Gotthardt K, Stieler J, Prange R.; ''γ2-Adaptin is functioning in the late endosomal sorting pathway and interacts with ESCRT-I and -III subunits.''; PubMed Europe PMC Scholia
20. Borner GH, Harbour M, Hester S, Lilley KS, Robinson MS.; ''Comparative proteomics of clathrin-coated vesicles.''; PubMed Europe PMC Scholia
21. Seaman MN, Sowerby PJ, Robinson MS.; ''Cytosolic and membrane-associated proteins involved in the recruitment of AP-1 adaptors onto the trans-Golgi network.''; PubMed Europe PMC Scholia
22. Burgos PV, Mardones GA, Rojas AL, daSilva LL, Prabhu Y, Hurley JH, Bonifacino JS.; ''Sorting of the Alzheimer's disease amyloid precursor protein mediated by the AP-4 complex.''; PubMed Europe PMC Scholia
23. Maier O, Knoblich M, Westermann P.; ''Dynamin II binds to the trans-Golgi network.''; PubMed Europe PMC Scholia
24. Verkerk AJ, Schot R, Dumee B, Schellekens K, Swagemakers S, Bertoli-Avella AM, Lequin MH, Dudink J, Govaert P, van Zwol AL, Hirst J, Wessels MW, Catsman-Berrevoets C, Verheijen FW, de Graaff E, de Coo IF, Kros JM, Willemsen R, Willems PJ, van der Spek PJ, Mancini GM.; ''Mutation in the AP4M1 gene provides a model for neuroaxonal injury in cerebral palsy.''; PubMed Europe PMC Scholia
25. Kirchhausen T.; ''Three ways to make a vesicle.''; PubMed Europe PMC Scholia
26. Aguilar RC, Boehm M, Gorshkova I, Crouch RJ, Tomita K, Saito T, Ohno H, Bonifacino JS.; ''Signal-binding specificity of the mu4 subunit of the adaptor protein complex AP-4.''; PubMed Europe PMC Scholia
27. Hirst J, Lindsay MR, Robinson MS.; ''GGAs: roles of the different domains and comparison with AP-1 and clathrin.''; PubMed Europe PMC Scholia
28. Farsad K, Ringstad N, Takei K, Floyd SR, Rose K, De Camilli P.; ''Generation of high curvature membranes mediated by direct endophilin bilayer interactions.''; PubMed Europe PMC Scholia
29. Abou Jamra R, Philippe O, Raas-Rothschild A, Eck SH, Graf E, Buchert R, Borck G, Ekici A, Brockschmidt FF, Nöthen MM, Munnich A, Strom TM, Reis A, Colleaux L.; ''Adaptor protein complex 4 deficiency causes severe autosomal-recessive intellectual disability, progressive spastic paraplegia, shy character, and short stature.''; PubMed Europe PMC Scholia
30. Rao SK, Huynh C, Proux-Gillardeaux V, Galli T, Andrews NW.; ''Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal exocytosis.''; PubMed Europe PMC Scholia
31. Guo Z, Turner C, Castle D.; ''Relocation of the t-SNARE SNAP-23 from lamellipodia-like cell surface projections regulates compound exocytosis in mast cells.''; PubMed Europe PMC Scholia

History

External references

DataNodes

Name	Type	Database reference	Comment
ADP	Metabolite	CHEBI:16761 (ChEBI)
AP-1 Complex	Complex	R-HSA-167717 (Reactome)
AP1B1	Protein	Q10567 (Uniprot-TrEMBL)
AP1G1	Protein	O43747 (Uniprot-TrEMBL)
AP1G2	Protein	O75843 (Uniprot-TrEMBL)
AP1G2:HGS:CHMP2A	Complex	R-HSA-5671700 (Reactome)
AP1G2	Protein	O75843 (Uniprot-TrEMBL)
AP1M1	Protein	Q9BXS5 (Uniprot-TrEMBL)
AP1M2	Protein	Q9Y6Q5 (Uniprot-TrEMBL)
AP1S1	Protein	P61966 (Uniprot-TrEMBL)
AP1S2	Protein	P56377 (Uniprot-TrEMBL)
AP1S3	Protein	Q96PC3 (Uniprot-TrEMBL)
AP3B1	Protein	O00203 (Uniprot-TrEMBL)
AP3S1	Protein	Q92572 (Uniprot-TrEMBL)
AP4:APP	Complex	R-HSA-5229081 (Reactome)
AP4:APP	Complex	R-HSA-5229085 (Reactome)
AP4B1	Protein	Q9Y6B7 (Uniprot-TrEMBL)
AP4E1	Protein	Q9UPM8 (Uniprot-TrEMBL)
AP4M1	Protein	O00189 (Uniprot-TrEMBL)
AP4	Complex	R-HSA-5229123 (Reactome)
AP4S1	Protein	Q9Y587 (Uniprot-TrEMBL)
APP(18-770)	Protein	P05067 (Uniprot-TrEMBL)
APP(18-770)	Protein	P05067 (Uniprot-TrEMBL)
ARF1	Protein	P84077 (Uniprot-TrEMBL)
ARRB1	Protein	P49407 (Uniprot-TrEMBL)
ARRB1	Protein	P49407 (Uniprot-TrEMBL)
ATP	Metabolite	CHEBI:15422 (ChEBI)
Arf1-GDP	Complex	R-HSA-201340 (Reactome)
Arf1-GTP	Complex	R-HSA-199981 (Reactome)
BLOC-1 Complex	Complex	R-HSA-429825 (Reactome)
BLOC1S1	Protein	P78537 (Uniprot-TrEMBL)
BLOC1S1	Protein	P78537 (Uniprot-TrEMBL)
BLOC1S3	Protein	Q6QNY0 (Uniprot-TrEMBL)
BLOC1S3	Protein	Q6QNY0 (Uniprot-TrEMBL)
BLOC1S4	Protein	Q9NUP1 (Uniprot-TrEMBL)
BLOC1S4	Protein	Q9NUP1 (Uniprot-TrEMBL)
BLOC1S6	Protein	Q9UL45 (Uniprot-TrEMBL)
BLOC1S6	Protein	Q9UL45 (Uniprot-TrEMBL)
CHMP2A	Protein	O43633 (Uniprot-TrEMBL)
CHMP2A	Protein	O43633 (Uniprot-TrEMBL)
CLAT:AP1:CLVS:PI(3,5)P2	Complex	R-HSA-5334658 (Reactome)
CLAT:AP1:CLVS	Complex	R-HSA-5333673 (Reactome)
CLINT1	Protein	Q14677 (Uniprot-TrEMBL)
CLINT1	Protein	Q14677 (Uniprot-TrEMBL)
CLTA	Protein	P09496 (Uniprot-TrEMBL)
CLTB	Protein	P09497 (Uniprot-TrEMBL)
CLTC	Protein	Q00610 (Uniprot-TrEMBL)
CLTC-1	Protein	Q00610-1 (Uniprot-TrEMBL)
CLVS1	Protein	Q8IUQ0 (Uniprot-TrEMBL)
CLVS2	Protein	Q5SYC1 (Uniprot-TrEMBL)
CPD	Protein	O75976 (Uniprot-TrEMBL)
CTSZ	Protein	Q9UBR2 (Uniprot-TrEMBL)
Cargo:AP-1:Arf1-GTP:beta-Arrestin-1:Vamp Complex	Complex	R-HSA-432669 (Reactome)
Cargo:AP-1:Beta-arrestin:Clathrin Triskelion:Vamp Complex	Complex	R-HSA-351198 (Reactome)
Cargo:AP-1:Beta-arrestin:Vamp:Clathrin Triskelion:Dynamin:Endophilin Complex	Complex	R-HSA-350825 (Reactome)
Clathrin Triskelion	Complex	R-HSA-350827 (Reactome)
Clathrin light chain	Protein	P09496-1 (Uniprot-TrEMBL)
DNAJC6	Protein	O75061 (Uniprot-TrEMBL)
DNASE2	Protein	O00115 (Uniprot-TrEMBL)
DNM2	Protein	P50570 (Uniprot-TrEMBL)
DNM2	Protein	P50570 (Uniprot-TrEMBL)
DTNBP1	Protein	Q96EV8 (Uniprot-TrEMBL)
DTNBP1	Protein	Q96EV8 (Uniprot-TrEMBL)
FTH1	Protein	P02794 (Uniprot-TrEMBL)
FTL	Protein	P02792 (Uniprot-TrEMBL)
Ferritin Complex	Complex	R-HSA-434350 (Reactome)	The ferritin complex is an oligomer of 24 subunits with light and heavy chains. The structural features of ferritin arise from the combination in various ratios of two subunits, H and L, which differ in size, amino acid composition, surface charge, and immunoreactivity. A corollary related differences in ferritin iron content to the functional efficiency of one of the two subunits for storing iron. In humans the H subunit is associated with a lower pI and lower iron content, and predominates in heart tissue, whereas the L subunit is associated with a higher pI and higher iron content, and predominates in the liver. The functional molecule forms a roughly spherical shell with a diameter of 12 nm and contains a central cavity into which the insoluble mineral iron core is deposited. Iron metabolism provides a useful example of gene expression translational control. Increased iron levels stimulate the synthesis of the iron-binding protein, ferritin, without any corresponding increase in the amount of ferritin mRNA. The 5'-UTR of both ferritin heavy chain mRNA and light chain mRNA contain a single iron-response element (IRE), a specific cis-acting regulatory sequence which forms a hairpin structure.
GAK	Protein	O14976 (Uniprot-TrEMBL)
GBF1	Protein	Q92538 (Uniprot-TrEMBL)
GDP	Metabolite	CHEBI:17552 (ChEBI)
GDP	Metabolite	CHEBI:17552 (ChEBI)
GNS	Protein	P15586 (Uniprot-TrEMBL)
GTP	Metabolite	CHEBI:15996 (ChEBI)
GTP	Metabolite	CHEBI:15996 (ChEBI)
Golgi-associated Vesicle Cargo	Complex	R-HSA-432672 (Reactome)
Golgi-associated Vesicle Cargo	Complex	R-HSA-435029 (Reactome)
Golgi-associated Vesicle Destined Cargo	Complex	R-HSA-432674 (Reactome)
Golgi-associated Vesicle Destined Cargo	Complex	R-HSA-435032 (Reactome)
Golgi-associated vesicle interacting proteins	Complex	R-HSA-434351 (Reactome)
HGS	Protein	O14964 (Uniprot-TrEMBL)
HGS	Protein	O14964 (Uniprot-TrEMBL)
HIP1R	Protein	O75146 (Uniprot-TrEMBL)
HSC70:Auxillin Complex	Complex	R-HSA-351175 (Reactome)
HSPA8	Protein	P11142 (Uniprot-TrEMBL)
IGF2R	Protein	P11717 (Uniprot-TrEMBL)
Lysosome Cargo:AP-1:Beta-arrestin:Clathrin Triskelion:Vamp Complex	Complex	R-HSA-432691 (Reactome)
Lysosome Destined Cargo:AP-1:Arf1-GTP:beta-Arrestin-1:Vamp Complex	Complex	R-HSA-432700 (Reactome)
Lysosome Destined Cargo:AP-1:Beta-arrestin:Vamp:Clathrin Triskelion:Dynamin:Endophilin Complex	Complex	R-HSA-432704 (Reactome)
Lysosome Cargo	Complex	R-HSA-432697 (Reactome)
Lysosome Cargo	Complex	R-HSA-435030 (Reactome)
Lysosome Destined Cargo	Complex	R-HSA-432690 (Reactome)
Lysosome Destined Cargo	Complex	R-HSA-435031 (Reactome)
M6PR	Protein	P20645 (Uniprot-TrEMBL)
NAPA	Protein	P54920 (Uniprot-TrEMBL)
NAPA	Protein	P54920 (Uniprot-TrEMBL)
NECAP1	Protein	Q8NC96 (Uniprot-TrEMBL)
OCRL	Protein	Q01968 (Uniprot-TrEMBL)
PI(3,5)P2	Metabolite	CHEBI:16851 (ChEBI)
PI(3,5)P2	Metabolite	CHEBI:16851 (ChEBI)
PICALM	Protein	Q13492 (Uniprot-TrEMBL)
PIK3C2A	Protein	O00443 (Uniprot-TrEMBL)
PUM1	Protein	Q14671 (Uniprot-TrEMBL)
PUM1	Protein	Q14671 (Uniprot-TrEMBL)
Pi	Metabolite	CHEBI:18367 (ChEBI)
RAB5C	Protein	P51148 (Uniprot-TrEMBL)
SH3D19	Protein	Q5HYK7 (Uniprot-TrEMBL)
SH3D19	Protein	Q5HYK7 (Uniprot-TrEMBL)
SH3GL2	Protein	Q99962 (Uniprot-TrEMBL)
SH3GL2	Protein	Q99962 (Uniprot-TrEMBL)
SNAP23	Protein	O00161 (Uniprot-TrEMBL)
SNAP23	Protein	O00161 (Uniprot-TrEMBL)
SNAPIN	Protein	O95295 (Uniprot-TrEMBL)
SNX2	Protein	O60749 (Uniprot-TrEMBL)
SNX5	Protein	Q9Y5X3 (Uniprot-TrEMBL)
SNX9	Protein	Q9Y5X1 (Uniprot-TrEMBL)
SORT1	Protein	Q99523 (Uniprot-TrEMBL)
STX4	Protein	Q12846 (Uniprot-TrEMBL)
STX4	Protein	Q12846 (Uniprot-TrEMBL)
TBC1D8B	Protein	Q0IIM8 (Uniprot-TrEMBL)
TFRC(1-760)	Protein	P02786 (Uniprot-TrEMBL)
TGOLN2	Protein	O43493 (Uniprot-TrEMBL)
TPD52	Protein	P55327 (Uniprot-TrEMBL)
TPD52L1	Protein	Q16890 (Uniprot-TrEMBL)
TXNDC5	Protein	Q8NBS9 (Uniprot-TrEMBL)
TXNDC5	Protein	Q8NBS9 (Uniprot-TrEMBL)
VAMP2	Protein	P63027 (Uniprot-TrEMBL)
VAMP2	Protein	P63027 (Uniprot-TrEMBL)
VAMP7	Protein	P51809 (Uniprot-TrEMBL)
VAMP7	Protein	P51809 (Uniprot-TrEMBL)
VAMP8	Protein	Q9BV40 (Uniprot-TrEMBL)
VAMP8	Protein	Q9BV40 (Uniprot-TrEMBL)
Vamp2:SNAP23:Syn4 Secretory granule docking and fusion complex	Complex	R-HSA-376372 (Reactome)
Vamp7:SNAP23:Syn4 Plasma membrane vesicle docking and fusion complex	Complex	R-HSA-376340 (Reactome)
Vamp8:SNAP23:Syn4 Secretory granule docking and fusion complex	Complex	R-HSA-376367 (Reactome)
Vamp	Complex	R-HSA-432668 (Reactome)
Vamp	Complex	R-HSA-432673 (Reactome)
Vamp	Complex	R-HSA-432694 (Reactome)
YIPF6	Protein	Q96EC8 (Uniprot-TrEMBL)

Annotated Interactions

Source	Target	Type	Database reference	Comment
	ADP	Arrow	R-HSA-421836 (Reactome)
	ADP	Arrow	R-HSA-432688 (Reactome)
	AP-1 Complex	Arrow	R-HSA-421836 (Reactome)
	AP-1 Complex	Arrow	R-HSA-432688 (Reactome)
AP-1 Complex			R-HSA-421833 (Reactome)
AP-1 Complex			R-HSA-432712 (Reactome)
	AP1G2:HGS:CHMP2A	Arrow	R-HSA-5671702 (Reactome)
AP1G2			R-HSA-5671702 (Reactome)
	AP4:APP	Arrow	R-HSA-5229111 (Reactome)
	AP4:APP	Arrow	R-HSA-5229132 (Reactome)
AP4:APP			R-HSA-5229111 (Reactome)
AP4:APP		mim-catalysis	R-HSA-5229111 (Reactome)
AP4			R-HSA-5229132 (Reactome)
APP(18-770)			R-HSA-5229132 (Reactome)
	ARRB1	Arrow	R-HSA-421836 (Reactome)
	ARRB1	Arrow	R-HSA-432688 (Reactome)
ARRB1			R-HSA-421833 (Reactome)
ARRB1			R-HSA-432712 (Reactome)
ATP			R-HSA-421836 (Reactome)
ATP			R-HSA-432688 (Reactome)
	Arf1-GDP	Arrow	R-HSA-421831 (Reactome)
	Arf1-GDP	Arrow	R-HSA-432706 (Reactome)
Arf1-GDP			R-HSA-350769 (Reactome)
	Arf1-GTP	Arrow	R-HSA-350769 (Reactome)
Arf1-GTP			R-HSA-421833 (Reactome)
Arf1-GTP			R-HSA-432712 (Reactome)
	BLOC-1 Complex	Arrow	R-HSA-429815 (Reactome)
BLOC1S1			R-HSA-429815 (Reactome)
BLOC1S3			R-HSA-429815 (Reactome)
BLOC1S4			R-HSA-429815 (Reactome)
BLOC1S6			R-HSA-429815 (Reactome)
CHMP2A			R-HSA-5671702 (Reactome)
	CLAT:AP1:CLVS:PI(3,5)P2	Arrow	R-HSA-5333658 (Reactome)
CLAT:AP1:CLVS			R-HSA-5333658 (Reactome)
CLINT1			R-HSA-434362 (Reactome)
	Cargo:AP-1:Arf1-GTP:beta-Arrestin-1:Vamp Complex	Arrow	R-HSA-421833 (Reactome)
Cargo:AP-1:Arf1-GTP:beta-Arrestin-1:Vamp Complex			R-HSA-421831 (Reactome)
	Cargo:AP-1:Beta-arrestin:Clathrin Triskelion:Vamp Complex	Arrow	R-HSA-421835 (Reactome)
Cargo:AP-1:Beta-arrestin:Clathrin Triskelion:Vamp Complex			R-HSA-421836 (Reactome)
	Cargo:AP-1:Beta-arrestin:Vamp:Clathrin Triskelion:Dynamin:Endophilin Complex	Arrow	R-HSA-421831 (Reactome)
Cargo:AP-1:Beta-arrestin:Vamp:Clathrin Triskelion:Dynamin:Endophilin Complex			R-HSA-421835 (Reactome)
Cargo:AP-1:Beta-arrestin:Vamp:Clathrin Triskelion:Dynamin:Endophilin Complex		mim-catalysis	R-HSA-421835 (Reactome)
	Clathrin Triskelion	Arrow	R-HSA-421836 (Reactome)
	Clathrin Triskelion	Arrow	R-HSA-432688 (Reactome)
Clathrin Triskelion			R-HSA-421831 (Reactome)
Clathrin Triskelion			R-HSA-432706 (Reactome)
	DNM2	Arrow	R-HSA-421835 (Reactome)
	DNM2	Arrow	R-HSA-432707 (Reactome)
DNM2			R-HSA-421831 (Reactome)
DNM2			R-HSA-432706 (Reactome)
DTNBP1			R-HSA-429815 (Reactome)
Ferritin Complex			R-HSA-434362 (Reactome)
GBF1		mim-catalysis	R-HSA-350769 (Reactome)
	GDP	Arrow	R-HSA-350769 (Reactome)
	GDP	Arrow	R-HSA-421835 (Reactome)
	GDP	Arrow	R-HSA-432707 (Reactome)
GTP			R-HSA-350769 (Reactome)
GTP			R-HSA-421835 (Reactome)
GTP			R-HSA-432707 (Reactome)
	Golgi-associated Vesicle Cargo	Arrow	R-HSA-421836 (Reactome)
Golgi-associated Vesicle Destined Cargo			R-HSA-421833 (Reactome)
	Golgi-associated vesicle interacting proteins	Arrow	R-HSA-434362 (Reactome)
HGS			R-HSA-5671702 (Reactome)
	HSC70:Auxillin Complex	Arrow	R-HSA-421836 (Reactome)
	HSC70:Auxillin Complex	Arrow	R-HSA-432688 (Reactome)
HSC70:Auxillin Complex			R-HSA-421836 (Reactome)
HSC70:Auxillin Complex			R-HSA-432688 (Reactome)
	Lysosome Cargo:AP-1:Beta-arrestin:Clathrin Triskelion:Vamp Complex	Arrow	R-HSA-432707 (Reactome)
Lysosome Cargo:AP-1:Beta-arrestin:Clathrin Triskelion:Vamp Complex			R-HSA-432688 (Reactome)
	Lysosome Destined Cargo:AP-1:Arf1-GTP:beta-Arrestin-1:Vamp Complex	Arrow	R-HSA-432712 (Reactome)
Lysosome Destined Cargo:AP-1:Arf1-GTP:beta-Arrestin-1:Vamp Complex			R-HSA-432706 (Reactome)
	Lysosome Destined Cargo:AP-1:Beta-arrestin:Vamp:Clathrin Triskelion:Dynamin:Endophilin Complex	Arrow	R-HSA-432706 (Reactome)
Lysosome Destined Cargo:AP-1:Beta-arrestin:Vamp:Clathrin Triskelion:Dynamin:Endophilin Complex			R-HSA-432707 (Reactome)
Lysosome Destined Cargo:AP-1:Beta-arrestin:Vamp:Clathrin Triskelion:Dynamin:Endophilin Complex		mim-catalysis	R-HSA-432707 (Reactome)
	Lysosome Cargo	Arrow	R-HSA-432688 (Reactome)
Lysosome Destined Cargo			R-HSA-432712 (Reactome)
NAPA			R-HSA-429815 (Reactome)
PI(3,5)P2			R-HSA-5333658 (Reactome)
PUM1			R-HSA-434362 (Reactome)
	Pi	Arrow	R-HSA-421831 (Reactome)
	Pi	Arrow	R-HSA-421835 (Reactome)
	Pi	Arrow	R-HSA-421836 (Reactome)
	Pi	Arrow	R-HSA-432688 (Reactome)
	Pi	Arrow	R-HSA-432706 (Reactome)
	Pi	Arrow	R-HSA-432707 (Reactome)
			R-HSA-350769 (Reactome)	ARF1 helps to recruit AP-1 to Golgi membrane. AP-1 is not alone in this process of establishing a docking complex at the trans-Golgi Network. This section of the Golgi membrane will be where the new vesicle will be built and loaded.
			R-HSA-376357 (Reactome)	The lysosomal vesicle is targeted to and fused with the plasma membrane, releasing its contents into the extracellular space.
			R-HSA-376364 (Reactome)	The vamp8 associated vesicle docks and fuses with the plasma membrane.
			R-HSA-376369 (Reactome)	The vamp2 associated vesicle docks and fuses with the plasma membrane.
			R-HSA-421831 (Reactome)	Once the basic components of the docking complex are assembled with one end of AP-1 bound to cargo molecules, the other end binds to clathrin. Clathrin triskelions polymerize into hexagons and pentagons, forming a cage, which leads to membrane deformation. This polymerization step drives the sculpting of the vesicle. The number of clathrin triskelions required to sculpt a vesicle appears to be variable, but has been estimated to require 36 - 60 triskelions assocaited with 30 - 66 AP-1 complexes. Here a ~380 angstroms vesicle is represented with 48 clathrin triskelions and 52 AP-1 complexes.
			R-HSA-421833 (Reactome)	Once AP-1 is recruited to the trans-Golgi Network membrane the complex of functional vesicle building proteins is joined by the cargo that will be within that vesicle. As with other types of vesicles the cargo itself is part of the vesicle development. Here the cargo is destined for the Golgi-associated vesicle membrane. It is at this stage that a specific Synaptobrevin (Vamp) molecule also joins the complex. It should be noted that only certain Vamp molecules will be found with specific cargo molecules on the newly forming vesicles. However here we represent this reaction in bulk, without specific Vamp and cargo molecule pairings.
			R-HSA-421835 (Reactome)	Dynamin is recruited to the growing vesicle and, under conditions that interfere with its GTPase activity, dynamin forms a collar or ring around the neck of the budding vesicle. It is unclear whether dynamin acts as a mechanochemical transducer to generate fission or as a recruiter to attach other proteins that are directly responsible for the fission step. Lipid-modifying enzymes such as endophilin are also involved in vesicle formation. Endophilin is an acyltransferase that interacts with dynamin and that generates lysophosphatidic acid. The current view is that this reaction produces a negative curvature at the neck of the vesicle.
			R-HSA-421836 (Reactome)	The heat shock protein Hsc70 and auxilin, a J-domain containing protein, are responsible for clathrin disassembly through an ATP-dependent reaction. This uncoating step may be a point in the pathway subject to regulation. This final step releases the vesicle from the clathrin cage. The vesicle still contatins a specific Vamp molecule, part of the targeting and fusion mechanism that delivers the vesicle to its ultimate destination. This vesicle also contains its cargo, membrane proteins embeded in the Golgi-associated vesicle membrane.
			R-HSA-429815 (Reactome)	The ubiquitously expressed protein complexes, named biogenesis of lysosome-related organelles complex or BLOC are required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.
			R-HSA-432688 (Reactome)	The heat shock protein Hsc70 and auxilin, a J-domain containing protein, are responsible for clathrin disassembly through an ATP-dependent reaction. This uncoating step may be a point in the pathway subject to regulation. This final step releases the vesicle from the clathrin cage. The vesicle still contatins a specific Vamp molecule, part of the targeting and fusion mechanism that delivers the vesicle to its ultimate destination. This vesicle also contains its cargo, membrane proteins embeded in the lysosome membrane.
			R-HSA-432706 (Reactome)	Once the basic components of the docking complex are assembled with one end of AP-1 bound to cargo molecules, the other end binds to clathrin. Clathrin triskelions polymerize into hexagons and pentagons, forming a cage, which leads to membrane deformation. This polymerization step drives the sculpting of the lysosome vesicle. Here only 5 clathrin triskelions are represented, though in reality many more would be involved in sculpting an entire vesicle.
			R-HSA-432707 (Reactome)	Dynamin is recruited to the growing lysosome destined vesicle and, under conditions that interfere with its GTPase activity, dynamin forms a collar or ring around the neck of the budding vesicle. It is unclear whether dynamin acts as a mechanochemical transducer to generate fission or as a recruiter to attach other proteins that are directly responsible for the fission step. Lipid-modifying enzymes such as endophilin are also involved in vesicle formation. Endophilin is an acyltransferase that interacts with dynamin and that generates lysophosphatidic acid. The current view is that this reaction produces a negative curvature at the neck of the vesicle.
			R-HSA-432712 (Reactome)	Once AP-1 is recruited to the trans-Golgi Network membrane the complex of functional vesicle building proteins is joined by the cargo that will be within that vesicle. As with other types of vesicles the cargo itself is part of the vesicle development. Here the cargo is destined for the lysosome membrane. It is at this stage that a specific Synaptobrevin (Vamp) molecule also joins the complex. It should be noted that only certain Vamp molecules will be found with specific cargo molecules on the newly forming vesicles. However here we represent this reaction in bulk, without specific Vamp and cargo molecule pairings.
			R-HSA-434362 (Reactome)	Cytosolic proteins are also recruited to the cyctoplasmic face of newly formed vesicles.
			R-HSA-5229111 (Reactome)	AP-4 complex subunit mu-1 (AP4M1) can recognise and interact with tyrosine-based (YXXphi) sorting signals found within the cytoplasmic tails of integral membrane proteins such as the amyloid precursor protein (APP), implicated in Alzheimer's disease. Once bound to AP4M1, APP is transported from the trans-Golgi network (TGN) to endosomes, thereby reducing amyloidogenic processing of the protein. Disruption of this interaction decreases localisation of APP to endosomes and enhances gamma-secretase-catalysed cleavage of APP to the pathogenic amyloid-beta peptide (Burgos et al. 2010).
			R-HSA-5229132 (Reactome)	The family of heterotetrameric adaptor protein (AP) complexes function as vesicle coat components, involved in targeting cargo proteins from post-Golgi compartments to the endosomal-lysosomal system. Adaptor protein 4 (AP4) is the most recently discovered and least characterised member of this family. AP4 consists of four subunits; two large adaptins (AP4E1 and AP4B1), a medium adaptin (AP4M1) and a small adaptin (AP4S1). The medium (mu) adaptins of all AP complexes can recognise and interact with tyrosine-based (YXXphi) sorting signals found within the cytoplasmic tails of integral membrane proteins (Aguilar et al. 2001, Hirst et al. 1999). The amyloid precursor protein (APP), implicated in Alzheimer's disease, contains such a signal in its cytoplasmic tail. It can therefore bind to AP4M1 of the AP4 complex and subsequently, be transported from the trans-Golgi network (TGN) to endosomes, thereby reducing amyloidogenic processing of the protein. Disruption of the this interaction decreases localisation of APP to endosomes and enhances gamma-secretase-catalysed cleavage of APP to the pathogenic amyloid-beta peptide (Burgos et al. 2010). Defects in AP4M1 can cause cerebral palsy, spastic quadriplegic 3 (CPSQ3; MIM:612936), a non-progressive disorder of movement and/or posture resulting from defects in CNS development (Verkerk et al. 2009). Defects in AP4S1 can cause cerebral palsy, spastic quadriplegic 6 (CPSQ6; MIM:614067), a neurodevelopmental disorder characterised by hypertonia and spasticity, and severe mental retardation with poor or absent speech development (Abou Jamra et al. 2011).
			R-HSA-5333658 (Reactome)	Clathrin-coated vesicles (CCVs) originating from the trans-Golgi network (TGN) provide a major transport pathway from the secretory system to endosomes/lysosomes. Clavesin 1 and 2 (CLVS1 and 2) are enriched on CCVs and form a complex with clathrin heavy chain (CHC) and adaptor protein-1 (AP1) complex, major coat components of TGN-derived CCVs. The complex can bind phosphatidylinositol 3,5-bisphosphate (PIP2), a phospholipid localised to late endosomes and lysosomes. This interaction is thought to assist the transport of cytosolic cargo proteins to the endosomal network (Katoh et al. 2009).
			R-HSA-5671702 (Reactome)	AP-1 complex subunit gamma-like 2 (AP1G2) is an 87-kDa protein that is similar to gamma-adaptin (AP1G1), a large chain of the AP1 clathrin-associated adaptor complex, both in primary structure (60% amino acid identity) and domain organisation (Takatsu et al. 1998). AP1G2 can be viewed as a putative endosomal sorting and trafficking adaptor that is specifically required for degradative endocytic trafficking and may help in maintaining homeostasis of the multivesicular body (MVB) protein-sorting pathway. AP1G2 specifically interacts with the core ESCRT subunits hepatocyte growth factor-regulated tyrosine kinase substrate (HGS, aka HRS) and charged multivesicular body protein 2a (CHMP2A aka hVps2-1), involved in MVB processing (Doring et al. 2010). AP1G2 is also able to bind the large envelope protein (surface protein S) of the hepatitis B virus (HBV), a protein that plays an important role in viral budding (Hartmann-Stuhler & Prange 2001). Disruption of this binding can inhibit virus production (Rost et al. 2006). Thus, AP1G2 may play a role in L-mediated processes of viral biogenesis or pathogenesis.
SH3D19			R-HSA-434362 (Reactome)
	SH3GL2	Arrow	R-HSA-421835 (Reactome)
	SH3GL2	Arrow	R-HSA-432707 (Reactome)
SH3GL2			R-HSA-421831 (Reactome)
SH3GL2			R-HSA-432706 (Reactome)
	SNAP23	Arrow	R-HSA-376357 (Reactome)
	SNAP23	Arrow	R-HSA-376364 (Reactome)
	SNAP23	Arrow	R-HSA-376369 (Reactome)
SNAP23			R-HSA-376357 (Reactome)
SNAP23			R-HSA-376364 (Reactome)
SNAP23			R-HSA-376369 (Reactome)
	STX4	Arrow	R-HSA-376357 (Reactome)
	STX4	Arrow	R-HSA-376364 (Reactome)
	STX4	Arrow	R-HSA-376369 (Reactome)
STX4			R-HSA-376357 (Reactome)
STX4			R-HSA-376364 (Reactome)
STX4			R-HSA-376369 (Reactome)
TXNDC5			R-HSA-429815 (Reactome)
	VAMP2	Arrow	R-HSA-376369 (Reactome)
VAMP2			R-HSA-376369 (Reactome)
	VAMP7	Arrow	R-HSA-376357 (Reactome)
VAMP7			R-HSA-376357 (Reactome)
	VAMP8	Arrow	R-HSA-376364 (Reactome)
VAMP8			R-HSA-376364 (Reactome)
Vamp2:SNAP23:Syn4 Secretory granule docking and fusion complex		mim-catalysis	R-HSA-376369 (Reactome)
Vamp7:SNAP23:Syn4 Plasma membrane vesicle docking and fusion complex		mim-catalysis	R-HSA-376357 (Reactome)
Vamp8:SNAP23:Syn4 Secretory granule docking and fusion complex		mim-catalysis	R-HSA-376364 (Reactome)
	Vamp	Arrow	R-HSA-421836 (Reactome)
	Vamp	Arrow	R-HSA-432688 (Reactome)
	Vamp	Arrow	R-HSA-434362 (Reactome)
Vamp			R-HSA-421833 (Reactome)
Vamp			R-HSA-432712 (Reactome)
Vamp			R-HSA-434362 (Reactome)