Protein folding (Homo sapiens)

From WikiPathways

Revision as of 13:51, 8 May 2014 by Anwesha (Talk | contribs)
Jump to: navigation, search
ArcPathVisio Brace Ellipse EndoplasmicReticulum GolgiApparatus HexagonPathVisio MimDegradation Mitochondria Octagon PentagonPathVisio Rectangle RoundedRectangle SarcoplasmicReticulum TriangleEquilateralEast TrianglePathVisio none cytosolPrefoldinPrefoldin-associated actin/tubulinPrefoldinunfolded actin/tubulinCCT/TriCactin/tubulin-bound CCT/TriCCCT/TriCunfolded actin/tubulinCCT/TriCCCT/TriCUnfolded alpha/beta tubulinCCT/TriCUnfolded alpha/beta tubulintubulin-GTP folding intermediatealpha/beta tubulin folding intermediatebeta-tubulin folding intermediatealpha-tubulin folding intermediateCCT/TriCCCT/TriCCCT/TriCCCT/TriCCCT/TriCCCT/TriCCCT/TriCsubstrate complexCCT/TriCGTPbeta-tubulin folding intermediatebeta-tubulin folding intermediatecofactor AGTPbeta-tubulin folding intermediateGTPbeta-tubulin folding intermediatebeta-tubulin folding intermediateCofactor DGTPbeta tubulinGTPbeta-tubulin folding intermediatebeta-tubulin folding intermediateGTP-alpha-tubulin folding intermediatealpha-tubulin folding intermediateCofactor BGTP-alpha tubulinGTP-alpha-tubulin folding intermediatealpha-tubulin folding intermediateCofactor EGTP-alpha tubulin foldingGTP-alpha-tubulin folding intermediatealpha-tubulin folding intermediatebeta tubulinGTP Cofactor Dalpha tubulinGTPCofactor ECofactor DGTPbeta tubulinGTPbeta-tubulin folding intermediatebeta-tubulin folding intermediateCofactor EGTP-alpha tubulin foldingGTP-alpha-tubulin folding intermediatealpha-tubulin folding intermediatebeta-tubulinGTPCofactor Dalpha-tubulinGTPCofactor E Cofactor Cbeta tubulinGTP Cofactor Dalpha tubulinGTPCofactor ECofactor DGTPbeta tubulinGTPbeta-tubulin folding intermediatebeta-tubulin folding intermediateCofactor EGTP-alpha tubulin foldingGTP-alpha-tubulin folding intermediatealpha-tubulin folding intermediatealpha-beta heterodimernative alpha tubulin-GTPnative beta-tubulinGTPbeta tubulinPrefoldinunfolded actin/tubulinPrefoldin-associated actin/tubulinCCT/TriCactin/tubulin-bound CCT/TriCATPCCT/TriCCCT/TriCADPGTPtubulin-GTP folding intermediatePiATPCCT/TriCCCT/TriCADPACTBPiSPHK1CCT/TriCCCT/TriC substrate proteins with unknown chaperonesCCT/TriCsubstrate complexTBCAGTPbeta-tubulin folding intermediatecofactor AGTPbeta-tubulin folding intermediateTBCDCofactor DGTPbeta tubulinGTP-alpha-tubulin folding intermediateTBCBCofactor BGTP-alpha tubulinTBCECofactor EGTP-alpha tubulin foldingbeta tubulinGTP Cofactor Dalpha tubulinGTPCofactor ETBCCbeta-tubulinGTPCofactor Dalpha-tubulinGTPCofactor E Cofactor Calpha-beta heterodimerPiPFDN1PFDN2VBP1PFDN4PFDN5PFDN6PFDN1PFDN2VBP1PFDN4PFDN5PFDN6Unfolded ACTBTUBA4A unfoldedTUBA1A unfoldedTUBA1C unfoldedTUBB1 unfoldedTUBB2A unfoldedTUBB2B unfoldedTUBB4B unfoldedTUBB3 unfoldedTUBB4A unfoldedTUBB6 unfoldedTUBA3C unfoldedTCP1CCT2CCT4CCT5CCT7CCT3CCT8CCT6AADPTCP1CCT2CCT4CCT5CCT7CCT3CCT8CCT6AADPUnfolded ACTBTUBA4A unfoldedTUBA1A unfoldedTUBA1C unfoldedTUBB1 unfoldedTUBB2A unfoldedTUBB2B unfoldedTUBB4B unfoldedTUBB3 unfoldedTUBB4A unfoldedTUBB6 unfoldedTUBA3C unfoldedTCP1CCT2CCT4CCT5CCT7CCT3CCT8CCT6AADPTUBA4A unfoldedTUBA1B unfoldedTUBA1A unfoldedTUBA1C unfoldedTUBB1 unfoldedTUBB2A unfoldedTUBB2B unfoldedTUBB4B unfoldedTUBB3 unfoldedTUBB4A unfoldedTUBB6 unfoldedTUBA3C unfoldedTCP1CCT2CCT4CCT5CCT7CCT3CCT8CCT6AATPTUBA4A unfoldedTUBA1B unfoldedTUBA1A unfoldedTUBA1C unfoldedTUBB1 unfoldedTUBB2A unfoldedTUBB2B unfoldedTUBB4B unfoldedTUBB3 unfoldedTUBB4A unfoldedTUBB6 unfoldedTUBA3C unfoldedGTPTUBB1 folding intermediateTUBB2A folding intermediateTUBB2B folding intermediateTUBB4B folding intermediateTUBB3 folding intermediateTUBB4A folding intermediateTUBB6 folding intermediateTUBA4A folding intermediateTUBA1A folding intermediateTUBA1C folding intermediateTUBA1B folding intermediateTUBA3C folding intermediateTCP1CCT2CCT4CCT5CCT7CCT3CCT8CCT6AADPUnfolded ACTBTCP1CCT2CCT4CCT5CCT7CCT3CCT8CCT6AATPUnfolded ACTBTCP1CCT2CCT4CCT5CCT7CCT3CCT8CCT6AADPSPHK1TCP1CCT2CCT4CCT5CCT7CCT3CCT8CCT6AADPGTPTUBB1 folding intermediateTUBB2A folding intermediateTUBB2B folding intermediateTUBB4B folding intermediateTUBB3 folding intermediateTUBB4A folding intermediateTUBB6 folding intermediateTBCAGTPTUBB1 folding intermediateTUBB2A folding intermediateTUBB2B folding intermediateTUBB4B folding intermediateTUBB3 folding intermediateTUBB4A folding intermediateTUBB6 folding intermediateGTPTUBB1 folding intermediateTUBB2A folding intermediateTUBB2B folding intermediateTUBB4B folding intermediateTUBB3 folding intermediateTUBB4A folding intermediateTUBB6 folding intermediateTBCDGTPTUBA4A folding intermediateTUBA1A folding intermediateTUBA1C folding intermediateTUBA1B folding intermediateTUBA3C folding intermediateGTPTUBA4A folding intermediateTUBA1A folding intermediateTUBA1C folding intermediateTUBA1B folding intermediateTUBA3C folding intermediateTBCBTBCEGTPTUBA4A folding intermediateTUBA1A folding intermediateTUBA1C folding intermediateTUBA1B folding intermediateTUBA3C folding intermediateGTPTUBB1 folding intermediateTUBB2A folding intermediateTUBB2B folding intermediateTUBB4B folding intermediateTUBB3 folding intermediateTUBB4A folding intermediateTUBB6 folding intermediateTBCDTBCETUBA4A folding intermediateTUBA1A folding intermediateTUBA1C folding intermediateTUBA1B folding intermediateTUBA3C folding intermediateGTPTUBB1 folding intermediateTUBB2A folding intermediateTUBB2B folding intermediateTUBB4B folding intermediateTUBB3 folding intermediateTUBB4A folding intermediateTUBB6 folding intermediateTBCDTBCETUBA4A folding intermediateTUBA1A folding intermediateTUBA1C folding intermediateTUBA1B folding intermediateTUBA3C folding intermediateTBCCGTPTUBB3TUBB4ATUBB4BTUBB2ATUBB1TUBB2BTUBB6Name: Protein foldingOrganism: Homo sapiens


Description

Due to the crowded envirnoment within the cell, many proteins must interact with molecular chaperones to attain their native conformation (reviewed in Young et al., 2004). Chaperones recognize and associate with proteins in their non-native state and facilitate their folding by stabilizing the conformation of productive folding intermediates. Chaperones that take part broadly in de novo protein folding, such as the Hsp70s and the chaperonins, facilitate the folding process through cycles of substrate binding and release regulated by their ATPase activity (see Young et al., 2004; Spiess et al., 2004; Bigotti and Clarke, 2008). Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=391251

Try the New WikiPathways

View approved pathways at the new wikipathways.org.

Quality Tags

Image:Reactome.pngCommunity: Reactome
Image:Unconnected.pngFix interactions

Ontology Terms

 

Bibliography

View all...
  1. Plimpton RL, Cuéllar J, Lai CW, Aoba T, Makaju A, Franklin S, Mathis AD, Prince JT, Carrascosa JL, Valpuesta JM, Willardson BM.; ''Structures of the Gβ-CCT and PhLP1-Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly.''; PubMed Europe PMC Scholia
  2. Freund A, Zhong FL, Venteicher AS, Meng Z, Veenstra TD, Frydman J, Artandi SE.; ''Proteostatic control of telomerase function through TRiC-mediated folding of TCAB1.''; PubMed Europe PMC Scholia
  3. Litterman N, Ikeuchi Y, Gallardo G, O'Connell BC, Sowa ME, Gygi SP, Harper JW, Bonni A.; ''An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi morphology and dendrite patterning.''; PubMed Europe PMC Scholia
  4. Kubota H, Hynes GM, Kerr SM, Willison KR.; ''Tissue-specific subunit of the mouse cytosolic chaperonin-containing TCP-1.''; PubMed Europe PMC Scholia
  5. Naletova IN, Popova KM, Eldarov MA, Kuravsky ML, Schmalhausen EV, Sevostyanova IA, Muronetz VI.; ''Chaperonin TRiC assists the refolding of sperm-specific glyceraldehyde-3-phosphate dehydrogenase.''; PubMed Europe PMC Scholia
  6. Lukov GL, Baker CM, Ludtke PJ, Hu T, Carter MD, Hackett RA, Thulin CD, Willardson BM.; ''Mechanism of assembly of G protein betagamma subunits by protein kinase CK2-phosphorylated phosducin-like protein and the cytosolic chaperonin complex.''; PubMed Europe PMC Scholia
  7. Bigotti MG, Clarke AR.; ''Chaperonins: The hunt for the Group II mechanism.''; PubMed Europe PMC Scholia
  8. Tian G, Lewis SA, Feierbach B, Stearns T, Rommelaere H, Ampe C, Cowan NJ.; ''Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors.''; PubMed Europe PMC Scholia
  9. Lu J, Chiang J, Iyer RR, Thompson E, Kaneski CR, Xu DS, Yang C, Chen M, Hodes RJ, Lonser RR, Brady RO, Zhuang Z.; ''Decreased glucocerebrosidase activity in Gaucher disease parallels quantitative enzyme loss due to abnormal interaction with TCP1 and c-Cbl.''; PubMed Europe PMC Scholia
  10. Young JC, Agashe VR, Siegers K, Hartl FU.; ''Pathways of chaperone-mediated protein folding in the cytosol.''; PubMed Europe PMC Scholia
  11. Yam AY, Xia Y, Lin HT, Burlingame A, Gerstein M, Frydman J.; ''Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly made proteins with complex topologies.''; PubMed Europe PMC Scholia
  12. Won KA, Schumacher RJ, Farr GW, Horwich AL, Reed SI.; ''Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT.''; PubMed Europe PMC Scholia
  13. Bhamidipati A, Lewis SA, Cowan NJ.; ''ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin.''; PubMed Europe PMC Scholia
  14. Lai CW, Kolesnikov AV, Frederick JM, Blake DR, Jiang L, Stewart JS, Chen CK, Barrow JR, Baehr W, Kefalov VJ, Willardson BM.; ''Phosducin-like protein 1 is essential for G-protein assembly and signaling in retinal rod photoreceptors.''; PubMed Europe PMC Scholia
  15. Lukov GL, Hu T, McLaughlin JN, Hamm HE, Willardson BM.; ''Phosducin-like protein acts as a molecular chaperone for G protein betagamma dimer assembly.''; PubMed Europe PMC Scholia
  16. Tracy CM, Kolesnikov AV, Blake DR, Chen CK, Baehr W, Kefalov VJ, Willardson BM.; ''Retinal cone photoreceptors require phosducin-like protein 1 for G protein complex assembly and signaling.''; PubMed Europe PMC Scholia
  17. Guenther MG, Yu J, Kao GD, Yen TJ, Lazar MA.; ''Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex.''; PubMed Europe PMC Scholia
  18. Howlett AC, Gray AJ, Hunter JM, Willardson BM.; ''Role of molecular chaperones in G protein beta5/regulator of G protein signaling dimer assembly and G protein betagamma dimer specificity.''; PubMed Europe PMC Scholia
  19. Wells CA, Dingus J, Hildebrandt JD.; ''Role of the chaperonin CCT/TRiC complex in G protein betagamma-dimer assembly.''; PubMed Europe PMC Scholia
  20. Melki R, Batelier G, Soulié S, Williams RC.; ''Cytoplasmic chaperonin containing TCP-1: structural and functional characterization.''; PubMed Europe PMC Scholia
  21. Miyata Y, Shibata T, Aoshima M, Tsubata T, Nishida E.; ''The molecular chaperone TRiC/CCT binds to the Trp-Asp 40 (WD40) repeat protein WDR68 and promotes its folding, protein kinase DYRK1A binding, and nuclear accumulation.''; PubMed Europe PMC Scholia
  22. Tian G, Thomas S, Cowan NJ.; ''Effect of TBCD and its regulatory interactor Arl2 on tubulin and microtubule integrity.''; PubMed Europe PMC Scholia
  23. Zebol JR, Hewitt NM, Moretti PA, Lynn HE, Lake JA, Li P, Vadas MA, Wattenberg BW, Pitson SM.; ''The CCT/TRiC chaperonin is required for maturation of sphingosine kinase 1.''; PubMed Europe PMC Scholia
  24. Spiess C, Meyer AS, Reissmann S, Frydman J.; ''Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.''; PubMed Europe PMC Scholia
  25. Trinidad AG, Muller PA, Cuellar J, Klejnot M, Nobis M, Valpuesta JM, Vousden KH.; ''Interaction of p53 with the CCT complex promotes protein folding and wild-type p53 activity.''; PubMed Europe PMC Scholia
  26. Kasembeli M, Lau WC, Roh SH, Eckols TK, Frydman J, Chiu W, Tweardy DJ.; ''Modulation of STAT3 folding and function by TRiC/CCT chaperonin.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
114801
Reactome
view16:29, 25 January 2021ReactomeTeamReactome version 75
113245view11:31, 2 November 2020ReactomeTeamReactome version 74
112464view15:41, 9 October 2020ReactomeTeamReactome version 73
101373view11:26, 1 November 2018ReactomeTeamreactome version 66
100911view21:01, 31 October 2018ReactomeTeamreactome version 65
100452view19:35, 31 October 2018ReactomeTeamreactome version 64
99999view16:19, 31 October 2018ReactomeTeamreactome version 63
99553view14:53, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93839view13:40, 16 August 2017ReactomeTeamreactome version 61
93394view11:22, 9 August 2017ReactomeTeamreactome version 61
88121view10:11, 26 July 2016RyanmillerOntology Term : 'protein folding pathway' added !
88120view10:10, 26 July 2016RyanmillerOntology Term : 'classic metabolic pathway' added !
86480view09:19, 11 July 2016ReactomeTeamreactome version 56
83103view09:59, 18 November 2015ReactomeTeamVersion54
81436view12:58, 21 August 2015ReactomeTeamVersion53
76909view08:18, 17 July 2014ReactomeTeamFixed remaining interactions
76614view11:59, 16 July 2014ReactomeTeamFixed remaining interactions
75945view10:00, 11 June 2014ReactomeTeamRe-fixing comment source
75647view10:53, 10 June 2014ReactomeTeamReactome 48 Update
75002view13:51, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74646view08:42, 30 April 2014ReactomeTeamReactome46
68999view17:45, 8 July 2013MaintBotUpdated to 2013 gpml schema
42108view21:57, 4 March 2011MaintBotAutomatic update
39918view05:56, 21 January 2011MaintBotNew pathway

External references

DataNodes

View all...
Name  ↓Type  ↓Database reference  ↓Comment  ↓
ACTBProteinP60709 (Uniprot-TrEMBL)
ADP MetaboliteCHEBI:16761 (ChEBI)
ADPMetaboliteCHEBI:16761 (ChEBI)
ATP MetaboliteCHEBI:15422 (ChEBI)
ATPMetaboliteCHEBI:15422 (ChEBI)
CCT/TriC substrate complexComplexREACT_17268 (Reactome)
CCT/TriC ComplexREACT_17090 (Reactome)
CCT/TriC substrate proteins with unknown chaperonesREACT_17376 (Reactome)
CCT/TriCComplexREACT_17102 (Reactome)
CCT/TriCComplexREACT_17160 (Reactome)
CCT/TriCComplexREACT_17874 (Reactome)
CCT/TriCComplexREACT_17889 (Reactome)
CCT/TriCComplexREACT_18085 (Reactome)
CCT2 ProteinP78371 (Uniprot-TrEMBL)
CCT3 ProteinP49368 (Uniprot-TrEMBL)
CCT4 ProteinP50991 (Uniprot-TrEMBL)
CCT5 ProteinP48643 (Uniprot-TrEMBL)
CCT6A ProteinP40227 (Uniprot-TrEMBL)
CCT7 ProteinQ99832 (Uniprot-TrEMBL)
CCT8 ProteinP50990 (Uniprot-TrEMBL)
Cofactor B GTP-alpha tubulinComplexREACT_17838 (Reactome)
Cofactor D

GTP

beta tubulin		ComplexREACT_17888 (Reactome)
Cofactor E GTP-alpha tubulin foldingComplexREACT_17474 (Reactome)
GTP beta-tubulin folding intermediateComplexREACT_18072 (Reactome)
GTP MetaboliteCHEBI:15996 (ChEBI)
GTP-alpha-tubulin folding intermediateComplexREACT_17776 (Reactome)
GTPMetaboliteCHEBI:15996 (ChEBI)
PFDN1ProteinO60925 (Uniprot-TrEMBL)
PFDN2 ProteinQ9UHV9 (Uniprot-TrEMBL)
PFDN4 ProteinQ9NQP4 (Uniprot-TrEMBL)
PFDN5ProteinQ99471 (Uniprot-TrEMBL)
PFDN6ProteinO15212 (Uniprot-TrEMBL)
PiMetaboliteCHEBI:18367 (ChEBI)
Prefoldin-associated actin/tubulinComplexREACT_18141 (Reactome)
PrefoldinComplexREACT_17255 (Reactome)
SPHK1 ProteinQ9NYA1 (Uniprot-TrEMBL)
SPHK1ProteinQ9NYA1 (Uniprot-TrEMBL)
TBCA ProteinO75347 (Uniprot-TrEMBL)
TBCAProteinO75347 (Uniprot-TrEMBL)
TBCB ProteinQ99426 (Uniprot-TrEMBL)
TBCBProteinQ99426 (Uniprot-TrEMBL)
TBCC ProteinQ15814 (Uniprot-TrEMBL)
TBCCProteinQ15814 (Uniprot-TrEMBL)
TBCD ProteinQ9BTW9 (Uniprot-TrEMBL)
TBCDProteinQ9BTW9 (Uniprot-TrEMBL)
TBCE ProteinQ15813 (Uniprot-TrEMBL)
TBCEProteinQ15813 (Uniprot-TrEMBL)
TCP1 ProteinP17987 (Uniprot-TrEMBL)
TUBA1A folding intermediate ProteinQ71U36 (Uniprot-TrEMBL)
TUBA1A unfolded ProteinQ71U36 (Uniprot-TrEMBL)
TUBA1B folding intermediate ProteinP68363 (Uniprot-TrEMBL)
TUBA1B unfolded ProteinP68363 (Uniprot-TrEMBL)
TUBA1C folding intermediate ProteinQ9BQE3 (Uniprot-TrEMBL)
TUBA1C unfolded ProteinQ9BQE3 (Uniprot-TrEMBL)
TUBA3C folding intermediate ProteinQ13748 (Uniprot-TrEMBL)
TUBA3C unfolded ProteinQ13748 (Uniprot-TrEMBL)
TUBA4A folding intermediate ProteinP68366 (Uniprot-TrEMBL)
TUBA4A unfolded ProteinP68366 (Uniprot-TrEMBL)
TUBB1 ProteinQ9H4B7 (Uniprot-TrEMBL)
TUBB1 folding intermediate ProteinQ9H4B7 (Uniprot-TrEMBL)
TUBB1 unfolded ProteinQ9H4B7 (Uniprot-TrEMBL)
TUBB2A ProteinQ13885 (Uniprot-TrEMBL)
TUBB2A folding intermediate ProteinQ13885 (Uniprot-TrEMBL)
TUBB2A unfolded ProteinQ13885 (Uniprot-TrEMBL)
TUBB2B ProteinQ9BVA1 (Uniprot-TrEMBL)
TUBB2B folding intermediate ProteinQ9BVA1 (Uniprot-TrEMBL)
TUBB2B unfolded ProteinQ9BVA1 (Uniprot-TrEMBL)
TUBB3 ProteinQ13509 (Uniprot-TrEMBL)
TUBB3 folding intermediate ProteinQ13509 (Uniprot-TrEMBL)
TUBB3 unfolded ProteinQ13509 (Uniprot-TrEMBL)
TUBB4A ProteinP04350 (Uniprot-TrEMBL)
TUBB4A folding intermediate ProteinP04350 (Uniprot-TrEMBL)
TUBB4A unfolded ProteinP04350 (Uniprot-TrEMBL)
TUBB4B ProteinP68371 (Uniprot-TrEMBL)
TUBB4B folding intermediate ProteinP68371 (Uniprot-TrEMBL)
TUBB4B unfolded ProteinP68371 (Uniprot-TrEMBL)
TUBB6 ProteinQ9BUF5 (Uniprot-TrEMBL)
TUBB6 folding intermediate ProteinQ9BUF5 (Uniprot-TrEMBL)
TUBB6 unfolded ProteinQ9BUF5 (Uniprot-TrEMBL)
Unfolded ACTB ProteinP60709 (Uniprot-TrEMBL)
VBP1 ProteinP61758 (Uniprot-TrEMBL)
actin/tubulin-bound CCT/TriCComplexREACT_17195 (Reactome)
alpha-beta heterodimerComplexREACT_18200 (Reactome)
beta tubulin

GTP 

Cofactor D

alpha tubulin GTP

Cofactor E		ComplexREACT_17650 (Reactome)
beta-tubulin

GTP Cofactor D alpha-tubulin GTP Cofactor E

Cofactor C		ComplexREACT_17144 (Reactome)
cofactor A

GTP

beta-tubulin folding intermediate		ComplexREACT_17443 (Reactome)
tubulin-GTP folding intermediateComplexREACT_17885 (Reactome)
unfolded actin/tubulinProteinREACT_17525 (Reactome)

Annotated Interactions

View all...
Source  ↓Target  ↓Type  ↓Database reference  ↓Comment  ↓
ACTBArrowREACT_16915 (Reactome)
ADPArrowREACT_16909 (Reactome)
ADPArrowREACT_17011 (Reactome)
ATPREACT_16909 (Reactome)
ATPREACT_17011 (Reactome)
CCT/TriC REACT_17011 (Reactome)
CCT/TriC substrate proteins with unknown chaperonesREACT_16984 (Reactome)
CCT/TriCArrowREACT_16909 (Reactome)
CCT/TriCArrowREACT_16915 (Reactome)
CCT/TriCArrowREACT_17011 (Reactome)
CCT/TriCArrowREACT_17032 (Reactome)
CCT/TriCREACT_16909 (Reactome)
CCT/TriCREACT_16961 (Reactome)
CCT/TriCREACT_16980 (Reactome)
CCT/TriCREACT_16984 (Reactome)
CCT/TriCREACT_17032 (Reactome)
Cofactor B GTP-alpha tubulinREACT_16937 (Reactome)
Cofactor D

GTP

beta tubulin		ArrowREACT_16986 (Reactome)
Cofactor D

GTP

beta tubulin		REACT_17060 (Reactome)
Cofactor E GTP-alpha tubulin foldingArrowREACT_16937 (Reactome)
Cofactor E GTP-alpha tubulin foldingREACT_17060 (Reactome)
GTP beta-tubulin folding intermediateREACT_16994 (Reactome)
GTP beta-tubulin folding intermediateREACT_17024 (Reactome)
GTP-alpha-tubulin folding intermediateREACT_16900 (Reactome)
GTP-alpha-tubulin folding intermediateREACT_17027 (Reactome)
GTPREACT_17032 (Reactome)
PiArrowREACT_16915 (Reactome)
PiArrowREACT_16958 (Reactome)
PiArrowREACT_17032 (Reactome)
Prefoldin-associated actin/tubulinREACT_16961 (Reactome)
PrefoldinArrowREACT_16961 (Reactome)
PrefoldinREACT_16892 (Reactome)
REACT_16892 (Reactome) During the synthesis of actin and tubulin, the nascent ribosome-associated chains bind to the heteromeric chaperone protein, prefoldin (PFD) (Hansen et al., 1999).
REACT_16900 (Reactome) Quasi-native alpha-tubulin folding intermediates generated via ATP-dependent interaction with CCT (Tian et al., 1995) are captured in a reversible reaction by cofactors B and/or E (Tian et al., 1997), forming the tubulin intermediate/cofactor complexes Factor B:alpha tubulin or Factor E:alpha tubulin.
REACT_16909 (Reactome) The interaction between CCT and unfolded target proteins is thought to occur when CCT is in its ADP-bound state. ADP is then exchanged for ATP in CCT.
REACT_16915 (Reactome) TriC/CCT-mediated beta-actin folding involves rapid ATP-independent formation of a binary complex, followed by a slower ATP-dependent release of the native product (Gao et al., 1992). Group II chaperonins enclose substrate proteins following substrate binding through the formation of a "built- in" lid over the central cavity. Upon ATP binding, lid formation is triggered by the transition state of ATP hydrolysis (Meyer, et al., 2003).
REACT_16937 (Reactome) The factor B:alpha tubulin complex act as a reservoir capable of accepting or delivering alpha tubulin to cofactor E (Tian et al., 1997). In the reverse reaction, cofactor B may displace cofactor E in the cofactor E:alpha tubulin complex.
REACT_16958 (Reactome) Beta tubulin within the active (Factor E:alpha tubulin: Factor D:beta tubulin:Factor C )-supercomplex hydrolyzes GTP. This results in the dissociation of the complex and the release of the native tubulin heterodimer (Tian et al., 1997).
REACT_16961 (Reactome) Unfolded actins and tubulins compete efficiently for binding to TriC/CCT and their chaperonin binding sites appear to be at least in part overlapping (Melki et al., 1993).
REACT_16980 (Reactome) CCT/TRiC facilitates folding of newly translated SK1 into its mature active form (Zebol et al., 2008)
REACT_16984 (Reactome) A combination of proteomic and bioinformatics analyses of TRiC substrates has revealed that they have complex topologies that are slow folding and aggregation prone (Yam et al., 2008). These substrates are also enriched in proteins that belong to oligomeric assemblies suggesting that TRiC plays a role in promoting complex assembly (Yam et al., 2008). Two possible mechanisms describing the role of TriC have been suggested (Yam et al., 2008). The processes of TRiC-mediated folding and assembly could be directly coupled, or TRiC could fold monomeric subunits and hold them in an assembly-competent state until they associate with the appropriate partner subunits. The complete list of TriC subsrates is not yet known. Many of its substrates that are targeted during biosynthesis are conserved between mammals and yeast (Yam et al. 2008).
REACT_16986 (Reactome) Factor A:beta tubulin complex act as a reservoir capable of accepting or delivering its target tubulin protein to cofactor D (Tian et al., 1997). In the reverse reaction, Cofactor A may displace cofactor D in a cofactor D:beta tubulin complex.
REACT_16994 (Reactome) Beta-tubulin folding intermediates generated via ATP-dependent interaction with TriC/CCT are captured by cofactors A and D (Tian et al., 1996; Tian et al., 1997) in a reversible reaction forming tubulin intermediate/cofactor complexes Factor A:beta tubulin or Factor D:beta tubulin.
REACT_17011 (Reactome) The interaction between CCT and unfolded target proteins is thought to occur when CCT is in its ADP-bound state. ADP is then exchanged for ATP in CCT.
REACT_17016 (Reactome) Entry of cofactor C to the factor E:alpha tubulin: factor D:beta tubulin complex generates the active alpha:beta-supercomplex (Tian et al., 1997).
REACT_17024 (Reactome) Beta-tubulin folding intermediates generated via ATP-dependent interaction with TriC/CCT are captured by cofactors A and D (Tian et al., 1996; Tian et al., 1997) in a reversible reaction forming tubulin intermediate/cofactor complexes Factor A:beta tubulin or Factor D:beta tubulin.
REACT_17027 (Reactome) Quasi-native alpha-tubulin folding intermediates generated via ATP-dependent interaction with CCT (Tian et al., 1995) are captured in a reversible reaction by cofactors B and/or E (Tian et al., 1997), forming the tubulin intermediate/cofactor complexes Factor B:alpha tubulin or Factor E:alpha tubulin.
REACT_17032 (Reactome) Group II chaperonins enclose substrate proteins following substrate binding through the formation of a "built- in" lid over the central cavity. Upon ATP binding, lid formation is triggered by the transition state of ATP hydrolysis (Meyer, et al., 2003). In the case of CCT-mediated tubulin folding, one or more rounds of ATP hydrolysis are likely required before the association of non-exchangeable GTP with chaperonin-bound alpha tubulin.
REACT_17060 (Reactome) Factor E:alpha tubulin and Factor D:beta tubulin interact with each other in a reversible reaction to form the complex (Factor E alpha tubulin:Factor D:beta tubulin) (Tian et al., 1997).
SPHK1REACT_16980 (Reactome)
TBCAArrowREACT_16986 (Reactome)
TBCAREACT_16994 (Reactome)
TBCBArrowREACT_16937 (Reactome)
TBCBREACT_16900 (Reactome)
TBCCArrowREACT_16958 (Reactome)
TBCCREACT_17016 (Reactome)
TBCDArrowREACT_16958 (Reactome)
TBCDREACT_16986 (Reactome)
TBCDREACT_17024 (Reactome)
TBCEArrowREACT_16958 (Reactome)
TBCEREACT_16937 (Reactome)
TBCEREACT_17027 (Reactome)
actin/tubulin-bound CCT/TriCArrowREACT_16961 (Reactome)
alpha-beta heterodimerArrowREACT_16958 (Reactome)
beta tubulin

GTP 

Cofactor D

alpha tubulin GTP

Cofactor E		REACT_17016 (Reactome)
cofactor A

GTP

beta-tubulin folding intermediate		REACT_16986 (Reactome)
tubulin-GTP folding intermediateArrowREACT_17032 (Reactome)
unfolded actin/tubulinREACT_16892 (Reactome)
Retrieved from "https://classic.wikipathways.org/index.php/Pathway:WP1892"
Personal tools