Activation of B‐Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601
dc.contributor.author | Zhang, Bao‐hong | en_US |
dc.contributor.author | Guan, Kun‐liang | en_US |
dc.date.accessioned | 2014-01-08T20:34:25Z | |
dc.date.available | 2014-01-08T20:34:25Z | |
dc.date.issued | 2000-10-16 | en_US |
dc.identifier.citation | Zhang, Bao‐hong ; Guan, Kun‐liang (2000). "Activation of Bâ Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601." The EMBO Journal 19(20): 5429-5439. <http://hdl.handle.net/2027.42/102072> | en_US |
dc.identifier.issn | 0261-4189 | en_US |
dc.identifier.issn | 1460-2075 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/102072 | |
dc.publisher | John Wiley & Sons, Ltd | en_US |
dc.subject.other | Phosphorylation | en_US |
dc.subject.other | Ras | en_US |
dc.subject.other | Kinase Activity | en_US |
dc.subject.other | B‐Raf | en_US |
dc.title | Activation of B‐Raf kinase requires phosphorylation of the conserved residues Thr598 and Ser601 | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Molecular, Cellular and Developmental Biology | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.identifier.pmid | 11032810 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/102072/1/emboj7593357.pdf | |
dc.identifier.doi | 10.1093/emboj/19.20.5429 | en_US |
dc.identifier.source | The EMBO Journal | en_US |
dc.identifier.citedreference | Shoji S, Ericsson LH, Walsh KA, Fischer EH and Titani K ( 1983 ) Amino acid sequence of the catalytic subunit of bovine type II adenosine cyclic 3′,5′‐phosphate dependent protein kinase. Biochemistry, 22, 3702 – 3709. | en_US |
dc.identifier.citedreference | Roy S, McPherson RA, Apolloni A, Yan J, Lane A, Clyde‐Smith J and Hancock JF ( 1998 ) 14‐3‐3 facilitates Ras‐dependent Raf‐1 activation in vitro and in vivo. Mol Cell Biol, 18, 3947 – 3955. | en_US |
dc.identifier.citedreference | Schlessinger J and Ullrich A ( 1992 ) Growth factor signaling by receptor tyrosine kinases. Neuron, 9, 383 – 391. | en_US |
dc.identifier.citedreference | Schramm K, Niehof M, Radziwill G, Rommel C and Moelling K ( 1994 ) Phosphorylation of c‐Raf‐1 by protein kinase A interferes with activation. Biochem Biophys Res Commun, 201, 740 – 747. | en_US |
dc.identifier.citedreference | Sternberg PW and Han M ( 1998 ) Genetics of RAS signaling in C.elegans. Trends Genet, 14, 466 – 472. | en_US |
dc.identifier.citedreference | Stewart S, Sundaram M, Zhang Y, Lee J, Han M and Guan KL ( 1999 ) Kinase suppressor of Ras forms a multiprotein signaling complex and modulates MEK localization. Mol Cell Biol, 19, 5523 – 5534. | en_US |
dc.identifier.citedreference | Sugimoto T, Stewart S, Han M and Guan KL ( 1998 ) The kinase suppressor of Ras (KSR) modulates growth factor and Ras signaling by uncoupling Elk‐1 phosphorylation from MAP kinase activation. EMBO J, 17, 1717 – 1727. | en_US |
dc.identifier.citedreference | Toker A and Newton AC ( 2000 ) Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK‐2 site. J Biol Chem, 275, 8271 – 8274. | en_US |
dc.identifier.citedreference | Tzivion G, Luo Z and Avruch J ( 1998 ) A dimeric 14‐3‐3 protein is an essential cofactor for Raf kinase activity. Nature, 394, 88 – 92. | en_US |
dc.identifier.citedreference | Vojtek AB, Hollenberg SM and Cooper JA ( 1993 ) Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell, 74, 205 – 214. | en_US |
dc.identifier.citedreference | Vossler MR, Yao H, York RD, Pan MG, Rim CS and Stork PJ ( 1997 ) cAMP activates MAP kinase and Elk‐1 through a B‐Raf‐ and Rap1‐dependent pathway. Cell, 89, 73 – 82. | en_US |
dc.identifier.citedreference | Weber CK, Slupsky JR, Herrmann C, Schuler M, Rapp UR and Block C ( 2000 ) Mitogenic signaling of Ras is regulated by differential interaction with Raf isozymes. Oncogene, 19, 169 – 176. | en_US |
dc.identifier.citedreference | Wojnowski L, Zimmer AM, Beck TW, Hahn H, Bernal R, Rapp UR and Zimmer A ( 1997 ) Endothelial apoptosis in Braf‐deficient mice [see comments]. Nature Genet, 16, 293 – 297. | en_US |
dc.identifier.citedreference | Wu J, Dent P, Jelinek T, Wolfman A, Weber MJ and Sturgill TW ( 1993 ) Inhibition of the EGF‐activated MAP kinase signaling pathway by adenosine 3′,5′‐monophosphate [see comments]. Science, 262, 1065 – 1069. | en_US |
dc.identifier.citedreference | Yao B, Zhang Y, Delikat S, Mathias S, Basu S and Kolesnick R ( 1995 ) Phosphorylation of Raf by ceramide‐activated protein kinase. Nature, 378, 307 – 310. | en_US |
dc.identifier.citedreference | Zhang Y et al. ( 1997 ) Kinase suppressor of Ras is ceramide‐activated protein kinase. Cell, 89, 63 – 72. | en_US |
dc.identifier.citedreference | Zheng CF and Guan KL ( 1994 ) Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues. EMBO J, 13, 1123 – 1131. | en_US |
dc.identifier.citedreference | Zimmermann S and Moelling K ( 1999 ) Phosphorylation and regulation of Raf by Akt (protein kinase B). Science, 286, 1741 – 1744. | en_US |
dc.identifier.citedreference | Alessi DR and Cohen P ( 1998 ) Mechanism of activation and function of protein kinase B. Curr Opin Genet Dev, 8, 55 – 62. | en_US |
dc.identifier.citedreference | Alessi DR, Saito Y, Campbell DG, Cohen P, Sithanandam G, Rapp U, Ashworth A, Marshall CJ and Cowley S ( 1994 ) Identification of the sites in MAP kinase kinase‐1 phosphorylated by p74raf‐1. EMBO J, 13, 1610 – 1619. | en_US |
dc.identifier.citedreference | Cai H, Smola U, Wixler V, Eisenmann‐Tappe I, Diaz‐Meco MT, Moscat J, Rapp U and Cooper GM ( 1997 ) Role of diacylglycerol‐regulated protein kinase C isotypes in growth factor activation of the Raf‐1 protein kinase. Mol Cell Biol, 17, 732 – 741. | en_US |
dc.identifier.citedreference | Carroll MP and May WS ( 1994 ) Protein kinase C‐mediated serine phosphorylation directly activates Raf‐1 in murine hematopoietic cells. J Biol Chem, 269, 1249 – 1256. | en_US |
dc.identifier.citedreference | Casamayor A, Morrice NA and Alessi DR ( 1999 ) Phosphorylation of Ser‐241 is essential for the activity of 3‐phosphoinositide‐dependent protein kinase‐1: identification of five sites of phosphorylation in vivo. Biochem J, 342, 287 – 292. | en_US |
dc.identifier.citedreference | Catling AD, Reuter CW, Cox ME, Parsons SJ and Weber MJ ( 1994 ) Partial purification of a mitogen‐activated protein kinase kinase activator from bovine brain. Identification as B‐Raf or a B‐Raf‐associated activity. J Biol Chem, 269, 30014 – 30021. | en_US |
dc.identifier.citedreference | Cook SJ and McCormick F ( 1993 ) Inhibition by cAMP of Ras‐dependent activation of Raf [see comments]. Science, 262, 1069 – 1072. | en_US |
dc.identifier.citedreference | Cutler RE,Jr, Stephens RM, Saracino MR and Morrison DK ( 1998 ) Autoregulation of the Raf‐1 serine/threonine kinase. Proc Natl Acad Sci USA, 95, 9214 – 9219. | en_US |
dc.identifier.citedreference | Daum G, Eisenmann‐Tappe I, Fries HW, Troppmair J and Rapp UR ( 1994 ) The ins and outs of Raf kinases. Trends Biochem Sci, 19, 474 – 480. | en_US |
dc.identifier.citedreference | English J, Pearson G, Wilsbacher J, Swantek J, Karandikar M, Xu S and Cobb MH ( 1999 ) New insights into the control of MAP kinase pathways. Exp Cell Res, 253, 255 – 270. | en_US |
dc.identifier.citedreference | Erhardt P, Schremser EJ and Cooper GM ( 1999 ) B‐Raf inhibits programmed cell death downstream of cytochrome c release from mitochondria by activating the MEK/Erk pathway. Mol Cell Biol, 19, 5308 – 5315. | en_US |
dc.identifier.citedreference | Fabian JR, Daar IO and Morrison DK ( 1993 ) Critical tyrosine residues regulate the enzymatic and biological activity of Raf‐1 kinase. Mol Cell Biol, 13, 7170 – 7179. | en_US |
dc.identifier.citedreference | Gorman C, Skinner RH, Skelly JV, Neidle S and Lowe PN ( 1996 ) Equilibrium and kinetic measurements reveal rapidly reversible binding of Ras to Raf. J Biol Chem, 271, 6713 – 6719. | en_US |
dc.identifier.citedreference | Grammatikakis N, Lin JH, Grammatikakis A, Tsichlis PN and Cochran BH ( 1999 ) p50(cdc37) acting in concert with Hsp90 is required for Raf‐1 function. Mol Cell Biol, 19, 1661 – 1672. | en_US |
dc.identifier.citedreference | Hagemann C and Rapp UR ( 1999 ) Isotype‐specific functions of Raf kinases. Exp Cell Res, 253, 34 – 46. | en_US |
dc.identifier.citedreference | Hill CS and Treisman R ( 1995 ) Transcriptional regulation by extracellular signals: mechanisms and specificity. Cell, 80, 199 – 211. | en_US |
dc.identifier.citedreference | Hughes K, Nikolakaki E, Plyte SE, Totty NF and Woodgett JR ( 1993 ) Modulation of the glycogen synthase kinase‐3 family by tyrosine phosphorylation. EMBO J, 12, 803 – 808. | en_US |
dc.identifier.citedreference | Inouye K, Mizutani S, Koide H and Kaziro Y ( 2000 ) Formation of the Ras dimer is essential for Raf‐1 activation. J Biol Chem, 275, 3737 – 3740. | en_US |
dc.identifier.citedreference | Jelinek T, Dent P, Sturgill TW and Weber MJ ( 1996 ) Ras‐induced activation of Raf‐1 is dependent on tyrosine phosphorylation [published erratum appears in Mol. Cell. Biol., 17, 2971, 1997]. Mol Cell Biol, 16, 1027 – 1034. | en_US |
dc.identifier.citedreference | King AJ, Sun H, Diaz B, Barnard D, Miao W, Bagrodia S and Marshall MS ( 1998 ) The protein kinase Pak3 positively regulates Raf‐1 activity through phosphorylation of serine 338. Nature, 396, 180 – 183. | en_US |
dc.identifier.citedreference | Kolch W, Heidecker G, Kochs G, Hummel R, Vahidi H, Mischak H, Finkenzeller G, Marme D and Rapp UR ( 1993 ) Protein kinase C α activates RAF‐1 by direct phosphorylation. Nature, 364, 249 – 252. | en_US |
dc.identifier.citedreference | Lewis TS, Shapiro PS and Ahn NG ( 1998 ) Signal transduction through MAP kinase cascades. Adv Cancer Res, 74, 49 – 139. | en_US |
dc.identifier.citedreference | MacNicol MC and MacNicol AM ( 1999 ) Nerve growth factor‐stimulated B‐Raf catalytic activity is refractory to inhibition by cAMP‐dependent protein kinase. J Biol Chem, 274, 13193 – 13197. | en_US |
dc.identifier.citedreference | MacNicol MC, Muslin AJ and MacNicol AM ( 2000 ) Disruption of the 14‐3‐3 binding site within the B‐Raf kinase domain uncouples catalytic activity from PC12 cell differentiation. J Biol Chem, 275, 3803 – 3809. | en_US |
dc.identifier.citedreference | Magnuson NS, Beck T, Vahidi H, Hahn H, Smola U and Rapp UR ( 1994 ) The Raf‐1 serine/threonine protein kinase. Semin Cancer Biol, 5, 247 – 253. | en_US |
dc.identifier.citedreference | Marshall CJ ( 1995 ) Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal‐regulated kinase activation. Cell, 80, 179 – 185. | en_US |
dc.identifier.citedreference | Mason CS, Springer CJ, Cooper RG, Superti‐Furga G, Marshall CJ and Marais R ( 1999 ) Serine and tyrosine phosphorylations cooperate in Raf‐1, but not B‐Raf activation. EMBO J, 18, 2137 – 2148. | en_US |
dc.identifier.citedreference | Michaud NR, Fabian JR, Mathes KD and Morrison DK ( 1995 ) 14‐3‐3 is not essential for Raf‐1 function: identification of Raf‐1 proteins that are biologically activated in a 14‐3‐3‐ and Ras‐independent manner. Mol Cell Biol, 15, 3390 – 3397. | en_US |
dc.identifier.citedreference | Mischak H, Seitz T, Janosch P, Eulitz M, Steen H, Schellerer M, Philipp A and Kolch W ( 1996 ) Negative regulation of Raf‐1 by phosphorylation of serine 621. Mol Cell Biol, 16, 5409 – 5418. | en_US |
dc.identifier.citedreference | Morrison DK and Cutler RE ( 1997 ) The complexity of Raf‐1 regulation. Curr Opin Cell Biol, 9, 174 – 179. | en_US |
dc.identifier.citedreference | Morrison DK, Heidecker G, Rapp UR and Copeland TD ( 1993 ) Identification of the major phosphorylation sites of the Raf‐1 kinase. J Biol Chem, 268, 17309 – 17316. | en_US |
dc.identifier.citedreference | Mott HR, Carpenter JW, Zhong S, Ghosh S, Bell RM and Campbell SL ( 1996 ) The solution structure of the Raf‐1 cysteine‐rich domain: a novel ras and phospholipid binding site. Proc Natl Acad Sci USA, 93, 8312 – 8317. | en_US |
dc.identifier.citedreference | Muslin AJ, Tanner JW, Allen PM and Shaw AS ( 1996 ) Interaction of 14‐3‐3 with signaling proteins is mediated by the recognition of phosphoserine. Cell, 84, 889 – 897. | en_US |
dc.identifier.citedreference | Nassar N, Horn G, Herrmann C, Scherer A, McCormick F and Wittinghofer A ( 1995 ) The 2.2 Å crystal structure of the Ras‐binding domain of the serine/threonine kinase c‐Raf1 in complex with Rap1A and a GTP analogue. Nature, 375, 554 – 560. | en_US |
dc.identifier.citedreference | Ohtsuka T, Shimizu K, Yamamori B, Kuroda S and Takai Y ( 1996 ) Activation of brain B‐Raf protein kinase by Rap1B small GTP‐binding protein. J Biol Chem, 271, 1258 – 1261. | en_US |
dc.identifier.citedreference | Payne DM, Rossomando AJ, Martino P, Erickson AK, Her JH, Shabanowitz J, Hunt DF, Weber MJ and Sturgill TW ( 1991 ) Identification of the regulatory phosphorylation sites in pp42/mitogen‐activated protein kinase (MAP kinase). EMBO J, 10, 885 – 892. | en_US |
dc.identifier.citedreference | Pritchard CA, Bolin L, Slattery R, Murray R and McMahon M ( 1996 ) Post‐natal lethality and neurological and gastrointestinal defects in mice with targeted disruption of the A‐Raf protein kinase gene. Curr Biol, 6, 614 – 617. | en_US |
dc.identifier.citedreference | Resing KA, Mansour SJ, Hermann AS, Johnson RS, Candia JM, Fukasawa K, Vande Woude GF and Ahn NG ( 1995 ) Determination of v‐Mos‐catalyzed phosphorylation sites and autophosphorylation sites on MAP kinase kinase by ESI/MS. Biochemistry, 34, 2610 – 2620. | en_US |
dc.identifier.citedreference | Reuter CW, Catling AD, Jelinek T and Weber MJ ( 1995 ) Biochemical analysis of MEK activation in NIH 3T3 fibroblasts. Identification of B‐Raf and other activators. J Biol Chem, 270, 7644 – 7655. | en_US |
dc.identifier.citedreference | Rommel C, Clarke BA, Zimmermann S, Nunez L, Rossman R, Reid K, Moelling K, Yancopoulos GD and Glass DJ ( 1999 ) Differentiation stage‐specific inhibition of the Raf‐MEK‐ERK pathway by Akt. Science, 286, 1738 – 1741. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.