Protein folding (Homo sapiens)

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1, 2, 4355alpha-tubulin folding intermediate CCT/TriCalpha-tubulin folding intermediate CCT/TriCtubulin-GTP folding intermediate CCT/TriCCCT/TriCunfolded actin/tubulin cofactor AGTPbeta-tubulin folding intermediate CCT/TriCCofactor EGTP-alpha tubulin folding GTPbeta-tubulin folding intermediate Unfolded alpha/beta tubulin alpha-tubulin folding intermediate GTPbeta-tubulin folding intermediate alpha-tubulin folding intermediate alpha-beta heterodimer GTPbeta-tubulin folding intermediate GTPbeta-tubulin folding intermediate native alpha tubulin-GTP alpha-tubulin folding intermediate CCT/TriCnative beta-tubulinGTP Prefoldin Prefoldin beta-tubulinGTPCofactor Dalpha-tubulinGTPCofactor E Cofactor C Unfolded alpha/beta tubulin CCT/TriCCofactor DGTPbeta tubulin beta-tubulin folding intermediate alpha/beta tubulin folding intermediate CCT/TriC beta-tubulin folding intermediate cytosolGTP-alpha-tubulin folding intermediate beta-tubulin folding intermediate CCT/TriCCCT/TriCbeta-tubulin folding intermediate GTP-alpha-tubulin folding intermediate GTP-alpha-tubulin folding intermediate Cofactor DGTPbeta tubulin Cofactor DGTPbeta tubulin CCT/TriCPrefoldin-associated actin/tubulin beta-tubulin folding intermediate GTP-alpha-tubulin folding intermediate beta tubulinGTP Cofactor Dalpha tubulinGTPCofactor E alpha-tubulin folding intermediate GTP-alpha-tubulin folding intermediate actin/tubulin-bound CCT/TriCCofactor EGTP-alpha tubulin folding beta tubulin Cofactor EGTP-alpha tubulin folding beta tubulinGTP Cofactor Dalpha tubulinGTPCofactor E CCT/TriCbeta-tubulin folding intermediate GTPbeta-tubulin folding intermediate CCT/TriCsubstrate complex unfolded actin/tubulin Cofactor BGTP-alpha tubulin CCT3 TUBA1A folding intermediate TUBB2B folding intermediate Unfolded ACTB PiTUBB2A folding intermediate ADP ATP ADPPFDN5TUBB4B folding intermediate CCT4 TUBA1C folding intermediate TUBA4A folding intermediate TUBA3C folding intermediate Cofactor EGTP-alpha tubulin foldingTCP1 TUBA1B folding intermediate PFDN1ADP TCP1 CCT7 TUBB6 folding intermediate TUBA4A unfolded PiCCT4 TUBB2B folding intermediate CCT5 TUBB4A TUBA1C folding intermediate TUBB2A unfolded CCT7 TBCBVBP1 TUBB6 unfolded GTP TUBA1B folding intermediate ADP TUBB1 folding intermediate CCT6A TUBB1 unfolded PFDN6TUBB4B folding intermediate TUBA1C folding intermediate TUBA1A folding intermediate TUBA1A folding intermediate CCT/TriCTUBB4B folding intermediate CCT/TriCCCT6A TUBA1C unfolded PFDN1TBCA TBCE CCT2 Cofactor BGTP-alpha tubulinTCP1 ACTBTBCD PFDN4 TUBB4A unfolded TUBB4B unfolded CCT5 CCT/TriC TUBB4B unfolded ADP CCT2 CCT8 TUBA4A folding intermediate TUBB3 folding intermediate Prefoldin-associated actin/tubulinTUBB1 folding intermediate TUBB4B folding intermediate GTP CCT7 CCT4 TUBB3 unfolded CCT8 TUBA4A folding intermediate TCP1 TBCB CCT8 TUBA1A unfolded TUBB2A folding intermediate TUBB4A unfolded CCT6A VBP1 TUBA1C unfolded TUBA4A folding intermediate CCT3 ATPTUBB6 folding intermediate TUBB2B folding intermediate GTP Unfolded ACTB TUBA3C folding intermediate GTP TUBB4A folding intermediate Unfolded ACTB TUBB6 folding intermediate CCT2 TUBB4A folding intermediate CCT2 TUBA1B folding intermediate TBCE TUBB1 unfolded TUBA1C folding intermediate CCT5 GTPbeta-tubulin folding intermediatePFDN4 TUBB1 folding intermediate TUBB3 folding intermediate TUBB3 folding intermediate Unfolded ACTB CCT8 TUBA1C unfolded CCT6A PFDN6TUBA1A unfolded TUBA1C unfolded cofactor AGTPbeta-tubulin folding intermediateSPHK1 TUBB3 folding intermediate TUBA3C folding intermediate GTP TUBB1 unfolded TUBB6 folding intermediate CCT4 TUBB6 TUBB4A folding intermediate TCP1 PFDN2 TUBB4A folding intermediate TUBA4A unfolded CCT7 CCT2 TUBB4A unfolded TUBB2B folding intermediate ADPTUBB2B folding intermediate TUBA1B unfolded TBCD CCT6A PFDN2 CCT/TriCCCT7 TUBB2A unfolded PiCCT7 TUBB1 folding intermediate CCT5 ATP TUBB3 folding intermediate TBCDTUBA1B folding intermediate TUBB4B unfolded TUBB2A unfolded TUBA4A folding intermediate CCT5 TUBA1A unfolded TUBB4B TUBB1 folding intermediate TBCE CCT4 CCT3 TUBB1 unfolded TUBB3 TUBB4A folding intermediate CCT8 GTP TUBB4B unfolded TUBB2A unfolded CCT6A TBCAADP beta-tubulinGTPCofactor Dalpha-tubulinGTPCofactor E Cofactor CCCT/TriCsubstrate complexCCT4 TUBA1A unfolded TBCECCT2 TUBB3 folding intermediate CCT6A TUBB4B folding intermediate CCT2 ADP TUBB2A folding intermediate TUBB3 unfolded TUBA1A folding intermediate ATPTUBB4A unfolded TUBB2A TUBB2A folding intermediate TUBB4B folding intermediate TUBB2B TBCC TUBA3C unfolded CCT7 TUBB6 folding intermediate TUBB6 unfolded CCT4 TUBA3C unfolded TUBB4A folding intermediate CCT3 TUBA1A folding intermediate TUBB3 unfolded CCT6A TUBA1B folding intermediate Cofactor DGTPbeta tubulinTUBB2B unfolded CCT5 TUBB2B unfolded PrefoldinTBCD TBCCTUBB2B unfolded CCT8 TUBB6 unfolded CCT3 TUBB1 folding intermediate CCT/TriCGTP CCT5 TUBB2B unfolded GTP TUBA1C folding intermediate TUBA4A unfolded TUBA1B folding intermediate TUBA1A folding intermediate CCT4 CCT2 GTP alpha-beta heterodimerCCT8 CCT3 CCT3 TUBB2A folding intermediate TUBB1 GTP-alpha-tubulin folding intermediateSPHK1TUBB3 unfolded TUBA1C folding intermediate tubulin-GTP folding intermediatePFDN5TUBA3C folding intermediate TCP1 TUBA4A unfolded TUBA3C unfolded TUBA1B unfolded TUBA3C folding intermediate CCT/TriC substrate proteins with unknown chaperonesTUBA3C unfolded CCT/TriCTCP1 CCT5 TUBB2A folding intermediate beta tubulinGTP Cofactor Dalpha tubulinGTPCofactor ECCT8 TUBB6 folding intermediate TCP1 TUBB6 unfolded actin/tubulin-bound CCT/TriCCCT3 unfolded actin/tubulinGTPGTP TUBB2B folding intermediate TUBA4A folding intermediate TUBA3C folding intermediate CCT7


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

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Bibliography

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  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
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  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
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  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
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  22. Tian G, Thomas S, Cowan NJ.; ''Effect of TBCD and its regulatory interactor Arl2 on tubulin and microtubule integrity.''; PubMed Europe PMC Scholia
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  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
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History

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CompareRevisionActionTimeUserComment
114801view16:29, 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...
NameTypeDatabase referenceComment
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...
SourceTargetTypeDatabase referenceComment
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"
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