RAF/MAP kinase cascade

Cseh B, Doma E, Baccarini M. “RAF” neighborhood: Protein–protein interaction in the Raf/Mek/Erk pathway. FEBS Letters. 2014 Jun 14;588(15):2398–406. doi: 10.1016/j.febslet.2014.06.025.; Roskoski R. ERK1/2 MAP kinases: structure, function, and regulation. Pharmacol Res. 2012 Aug;66(2):105–43. doi: 10.1016/j.phrs.2012.04.005. PMID: 22569528.; Kyriakis JM, Avruch J. Mammalian MAPK signal transduction pathways activated by stress and inflammation: a 10-year update. Physiol Rev. 2012 Apr;92(2):689–737. doi: 10.1152/physrev.00028.2011. PMID: 22535895.; Roskoski R. MEK1/2 dual-specificity protein kinases: Structure and regulation. Biochemical and Biophysical Research Communications. 2012 Jan;417(1):5–10. doi: 10.1016/j.bbrc.2011.11.145.; Plotnikov A, Zehorai E, Procaccia S, Seger R. The MAPK cascades: Signaling components, nuclear roles and mechanisms of nuclear translocation. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 2011 Sep;1813(9):1619–33. doi: 10.1016/j.bbamcr.2010.12.012.; Cantwell-Dorris ER, O'Leary JJ, Sheils OM. BRAFV600E: implications for carcinogenesis and molecular therapy. Mol Cancer Ther. 2011 Mar;10(3):385–94. doi: 10.1158/1535-7163.mct-10-0799. PMID: 21388974.; Cargnello M, Roux PP. Activation and function of the MAPKs and their substrates, the MAPK-activated protein kinases. Microbiol Mol Biol Rev. 2011 Mar;75(1):50–83. PMID: 21372320; PMCID: PMC3063353.; Roskoski R. RAF protein-serine/threonine kinases: Structure and regulation. Biochemical and Biophysical Research Communications. 2010 Aug;399(3):313–7. doi: 10.1016/j.bbrc.2010.07.092.; Brown MD, Sacks DB. Protein scaffolds in MAP kinase signalling. Cellular Signalling. 2009 Apr;21(4):462–9. doi: 10.1016/j.cellsig.2008.11.013.; McKay MM, Morrison DK. Integrating signals from RTKs to ERK/MAPK. Oncogene. 2007 May 14;26(22):3113–21. doi: 10.1038/sj.onc.1210394. PMID: 17496910.; Turjanski AG, Vaqué JP, Gutkind JS. MAP kinases and the control of nuclear events. Oncogene. 2007 May 14;26(22):3240–53. doi: 10.1038/sj.onc.1210415. PMID: 17496919.; Roberts PJ, Der CJ. Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer. Oncogene. 2007 May 14;26(22):3291–310. doi: 10.1038/sj.onc.1210422. PMID: 17496923.; Wellbrock C, Karasarides M, Marais R. The RAF proteins take centre stage. Nature Reviews Molecular Cell Biology. 2004 Nov;5(11):875–85. doi: 10.1038/nrm1498.; Davies H, Bignell GR, Cox C, Stephens P, Edkins S, Clegg S, Teague J, Woffendin H, Garnett MJ, Bottomley W, Davis N, Dicks E, Ewing R, Floyd Y, Gray K, Hall S, Hawes R, Hughes J, Kosmidou V, Menzies A, Mould C, Parker A, Stevens C, Watt S, Hooper S, Wilson R, Jayatilake H, Gusterson BA, Cooper C, Shipley J, Hargrave D, Pritchard-Jones K, Maitland N, Chenevix-Trench G, Riggins GJ, Bigner DD, Palmieri G, Cossu A, Flanagan A, Nicholson A, Ho JW, Leung SY, Yuen ST, Weber BL, Seigler HF, Darrow TL, Paterson H, Marais R, Marshall CJ, Wooster R, Stratton MR, Futreal PA. Mutations of the BRAF gene in human cancer. Nature. 2002 Jun 27;417(6892):949–54. doi: 10.1038/nature00766. PMID: 12068308.

Metabolites

Calcium cation

Formula: Ca (39.962591)

CAS ID: 14127-61-8

H2O

Formula: H2O (18.0105642)

CAS ID: 7732-18-5

Zinc cation

Formula: Zn (63.929145)

CAS ID: 23713-49-7

hexadecanoate

Formula: C16H31O2 (255.2323926)

CAS ID: 143-20-4

palmitoyl-CoA(4-)

Formula: C37H62N7O17P3S (1001.3135592)

CAS ID: 1763-10-6

ATP(4-)

Formula: C10H12N5O13P3 (502.9644492)

CAS ID:

GTP(4-)

Formula: C10H12N5O14P3 (518.9593642)

CAS ID: 86527-72-2

ADP(3-)

Formula: C10H12N5O10P2 (424.0059412)

CAS ID:

Palmostatin B

Formula: C23H36O4 (376.2613456)

CAS ID:

Cysmethynil

Formula: C25H32N2O (376.25145019999997)

CAS ID: 851636-83-4



Enzyme

EC Number name full name note
2.1.1.100 protein-S-isoprenylcysteine O-methyltransferase S-adenosyl-L-methionine:protein-C-terminal-S-farnesyl-L-cysteine O-methyltransferase
2.3.1.225 protein S-acyltransferase palmitoyl-CoA:[protein]-L-cysteine S-palmitoyltransferase
2.3.2.27 RING-type E3 ubiquitin transferase [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming; RING-type)
2.3.2.32 cullin-RING-type E3 NEDD8 transferase [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-yl-L-cysteine:[cullin] [NEDD8-protein] transferase (isopeptide bond-forming; RING-type)
2.5.1.58 protein farnesyltransferase farnesyl-diphosphate:protein-cysteine farnesyltransferase
2.5.1.59 protein geranylgeranyltransferase type I geranylgeranyl-diphosphate:protein-cysteine geranyltransferase
2.7.11.1 non-specific serine/threonine protein kinase ATP:protein phosphotransferase (non-specific)
2.7.11.13 protein kinase C ATP:protein phosphotransferase (diacylglycerol-dependent)
2.7.11.24 mitogen-activated protein kinase ATP:protein phosphotransferase (MAPKK-activated)
2.7.11.25 mitogen-activated protein kinase kinase kinase ATP:protein phosphotransferase (MAPKKKK-activated)
2.7.12.2 mitogen-activated protein kinase kinase ATP:protein phosphotransferase (MAPKKK-activated)
3.1.3.16 protein-serine/threonine phosphatase protein-serine/threonine-phosphate phosphohydrolase
3.1.3.48 protein-tyrosine-phosphatase protein-tyrosine-phosphate phosphohydrolase
3.4.19.12 ubiquitinyl hydrolase 1
3.4.26.1 intramembrane prenyl-peptidase Rce1
3.6.5.2 small monomeric GTPase GTP phosphohydrolase (cell-regulating)


Proteins

Protein ID name full name