Protein folding (Homo sapiens)

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212cytosolADPADPATPbeta-tubulin:GTP:Cofactor D:alpha-tubulin:GTP:Cofactor E : Cofactor CPrefoldinbeta-actinGTPATPbeta tubulin:GTP: Cofactor D:alpha tubulin:GTP:Cofactor ECCT/TriC (ADP) associated actinCCT/TriC(ADP)-associated non-native tubulinCCT/TriC(ATP)-associated actinTubulin-folding cofactor CPrefoldin-associated actin/tubulinCofactor D:GTP:beta tubulinOrthophosphateTubulin-folding cofactor Dtubulin-GTP folding intermediateCofactor E:GTP-alpha tubulin foldingOrthophosphateTubulin-folding cofactor BGTP:beta-tubulin folding intermediateactin/tubulin-bound CCT/TriC(ADP)alpha-beta heterodimerCCT/TriC:substrate complexTubulin-folding cofactor ECofactor B:GTP-alpha tubulinCCT/TriC(ATP):unfolded tubulin complexunfolded actin/tubulinSphingosine kinase 1OrthophosphateCCT/TriC(ADP)GTP-alpha-tubulin folding intermediateCCT/TriC substrate proteins with unknown chaperonescofactor A:GTP:beta-tubulin folding intermediateTubulin-folding cofactor ACCT/TriC(ADP):Sphingosine kinase 1


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).

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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
  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

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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
ADP Metabolite16761 (ChEBI)
ATP Metabolite15422 (ChEBI)
CCT/TriC (ADP)

associated actin

ComplexREACT_17090 (Reactome)
CCT/TriC substrate

proteins with unknown chaperones

REACT_17376 (Reactome)
CCT/TriC(ADP) ComplexREACT_17874 (Reactome)
CCT/TriC(ADP)-

associated non-native tubulin

ComplexREACT_17102 (Reactome)
CCT/TriC(ADP):

Sphingosine kinase 1

ComplexREACT_18085 (Reactome)
CCT/TriC(ATP)-

associated actin

ComplexREACT_17160 (Reactome)
CCT/TriC(ATP):

unfolded tubulin complex

ComplexREACT_17889 (Reactome)
CCT/TriC:substrate

complex

ComplexREACT_17268 (Reactome)
Cofactor B:

GTP-alpha tubulin

ComplexREACT_17838 (Reactome)
Cofactor D:GTP:beta

tubulin

ComplexREACT_17888 (Reactome)
Cofactor E:GTP-

alpha tubulin folding

ComplexREACT_17474 (Reactome)
GTP Metabolite15996 (ChEBI)
GTP-alpha-tubulin

folding intermediate

ComplexREACT_17776 (Reactome)
GTP:beta-tubulin

folding intermediate

ComplexREACT_18072 (Reactome)
Orthophosphate Metabolite18367 (ChEBI)
Prefoldin ComplexREACT_17255 (Reactome)
Prefoldin-associated

actin/tubulin

ComplexREACT_18141 (Reactome)
Sphingosine

kinase 1

ProteinQ9NYA1 (UniProt)
Tubulin-folding

cofactor A

ProteinO75347 (UniProt)
Tubulin-folding

cofactor B

ProteinQ99426 (UniProt)
Tubulin-folding

cofactor C

ProteinQ15814 (UniProt)
Tubulin-folding

cofactor D

ProteinQ9BTW9 (UniProt)
Tubulin-folding

cofactor E

ProteinQ15813 (UniProt)
actin/tubulin-

bound CCT/TriC (ADP)

ComplexREACT_17195 (Reactome)
alpha-beta

heterodimer

ComplexREACT_18200 (Reactome)
beta tubulin:GTP:

Cofactor D:alpha tubulin:GTP:Cofactor E

ComplexREACT_17650 (Reactome)
beta-actin ProteinP60709 (UniProt)
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

intermediate

ComplexREACT_17885 (Reactome)
unfolded

actin/tubulin

ProteinREACT_17525 (Reactome)

Annotated Interactions

No annotated interactions

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