Wavelength-specific Activation of MAP Kinase Family Proteins by Monochromatic UV Irradiation¶

2001 ◽  
Vol 73 (2) ◽  
pp. 147 ◽  
Author(s):  
Yukihito Kabuyama ◽  
Miwako K. Homma ◽  
Masayuki Sekimata ◽  
Yoshimi Homma
2007 ◽  
Vol 73 (2) ◽  
pp. 147-152
Author(s):  
Yukihito Kabuyama ◽  
Miwako K. Homma ◽  
Masayuki Sekimata ◽  
Yoshimi Homma

1998 ◽  
Vol 76 ◽  
pp. 65
Author(s):  
Noriyasu Hirasawa ◽  
Yuko Fujita ◽  
Yukako Sato ◽  
Suetsugu Mue ◽  
Kazuo Ohuchi
Keyword(s):  

2002 ◽  
Vol 8 (12) ◽  
pp. 857-862 ◽  
Author(s):  
Walter L. Vervenne ◽  
Carina L. Bos ◽  
Linda S. Rens ◽  
Maikel P. Peppelenbosch ◽  
Dick J. Richel

2001 ◽  
Vol 359 (3) ◽  
pp. 497-505 ◽  
Author(s):  
Sunke HIMPEL ◽  
Pascal PANZER ◽  
Klaus EIRMBTER ◽  
Hanna CZAJKOWSKA ◽  
Muhammed SAYED ◽  
...  

Protein kinases of the DYRK (‘dual-specificity tyrosine-regulated kinase’) family are characterized by a conserved Tyr-Xaa-Tyr motif (Tyr-319–Tyr-321) in a position exactly corresponding to the activation motif of the mitogen-activated protein kinase (MAP kinase) family (Thr-Xaa-Tyr). In a molecular model of the catalytic domain of DYRK1A, the orientation of phosphorylated Tyr-321 is strikingly similar to that of Tyr-185 in the known structure of the activated MAP kinase, extracellular-signal-regulated kinase 2. Consistent with our model, substitution of Tyr-321 but not of Tyr-319 by phenylalanine markedly reduced the enzymic activity of recombinant DYRK1A expressed in either Escherichia coli or mammalian cells. Direct identification of phosphorylated residues by tandem MS confirmed that Tyr-321, but not Tyr-319, was phosphorylated. When expressed in COS-7 cells, DYRK1A was found to be fully phosphorylated on Tyr-321. A catalytically inactive mutant of DYRK1A contained no detectable phosphotyrosine, indicating that Tyr-321 is autophosphorylated by DYRK1A. MS identified Tyr-111 and Ser-97 as additional autophosphorylation sites in the non-catalytic N-terminal domain of bacterially expressed DYRK1A. Enzymic activity was not affected in the DYRK1A-Y111F mutant. The present experimental data and the molecular model indicate that the activity of DYRK1A is dependent on the autophosphorylation of a conserved tyrosine residue in the activation loop.


2003 ◽  
Vol 89 (5) ◽  
pp. 863-867 ◽  
Author(s):  
Masahiro Eguchi ◽  
Mayumi Fujiwara ◽  
Yoichi Mizukami ◽  
Nobuhiko Miwa

1998 ◽  
Vol 5 (6) ◽  
pp. 321-328 ◽  
Author(s):  
Patrick A. Eyers ◽  
Molly Craxton ◽  
Nick Morricel ◽  
Philip Cohen ◽  
Michel Goedert

2000 ◽  
Vol 36 ◽  
pp. 105 ◽  
Author(s):  
J.M.W. Gee ◽  
J.F.R. Robertson ◽  
I.O. Ellis ◽  
R.I. Nicholson

1996 ◽  
Vol 21 (6) ◽  
pp. 771-781 ◽  
Author(s):  
Yusen Liu ◽  
Kathryn Z. Guyton ◽  
Myriam Gorospe ◽  
Qingbo Xu ◽  
John C. Lee ◽  
...  

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