A reevaluation of the spleen tyrosine kinase (SYK) activation mechanism.
ITAM (immune-receptor tyrosine activation motif)
autophosphorylation
cell signaling
conformational change
enzyme activation
enzyme kinetics
immunity
non-receptor tyrosine kinase (nRTK)
phosphorylation
spleen tyrosine kinase (SYK)
tonic signalling
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
10 05 2019
10 05 2019
Historique:
received:
15
02
2019
revised:
25
03
2019
pubmed:
30
3
2019
medline:
18
12
2019
entrez:
30
3
2019
Statut:
ppublish
Résumé
Spleen tyrosine kinase (SYK) is a signaling node in many immune pathways and comprises two tandem Src homology (SH) 2 domains, an SH2-kinase linker, and a C-terminal tyrosine kinase domain. Two prevalent models of SYK activation exist. The "OR-gate" model contends that SYK can be fully activated by phosphorylation or binding of its SH2 domains to a dual-phosphorylated immune-receptor tyrosine-based activation motif (ppITAM). An alternative model proposes that SYK activation requires ppITAM binding and phosphorylation of the SH2-kinase linker by a SRC family kinase such as LYN proto-oncogene, SRC family tyrosine kinase (LYN). To evaluate these two models, we generated directly comparable unphosphorylated (upSYK) and phosphorylated (pSYK) proteins with or without an N-terminal glutathione
Identifiants
pubmed: 30923129
pii: S0021-9258(20)35462-4
doi: 10.1074/jbc.RA119.008045
pmc: PMC6514621
doi:
Substances chimiques
MAS1 protein, human
0
Proto-Oncogene Mas
0
SYK protein, human
EC 2.7.10.2
Syk Kinase
EC 2.7.10.2
lyn protein-tyrosine kinase
EC 2.7.10.2
src-Family Kinases
EC 2.7.10.2
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
7658-7668Informations de copyright
© 2019 Mansueto et al.
Références
Nat Methods. 2005 Apr;2(4):277-83
pubmed: 15782220
Trends Pharmacol Sci. 2014 Aug;35(8):414-22
pubmed: 24975478
J Immunol. 1998 Nov 15;161(10):5276-83
pubmed: 9820500
J Pharmacol Exp Ther. 2006 May;317(2):571-8
pubmed: 16452391
J Am Soc Mass Spectrom. 2007 Feb;18(2):226-33
pubmed: 17070068
Biochemistry. 2007 Dec 25;46(51):15103-14
pubmed: 18052078
Nat Rev Immunol. 2006 Apr;6(4):283-94
pubmed: 16557260
J Mol Biol. 1990 May 20;213(2):221-2
pubmed: 2342105
Immunity. 2005 Jan;22(1):9-18
pubmed: 15664155
J Biol Chem. 2018 Mar 30;293(13):4591-4602
pubmed: 29440271
Science. 2003 Sep 26;301(5641):1904-8
pubmed: 14512628
Anal Chem. 1998 Sep 1;70(17):3557-65
pubmed: 9737207
J Biol Chem. 2011 Jul 22;286(29):25872-81
pubmed: 21602568
Mol Cell Biol. 2013 Jun;33(11):2188-201
pubmed: 23530057
Biochim Biophys Acta. 2009 Jul;1793(7):1115-27
pubmed: 19306898
J Immunol. 1998 Oct 15;161(8):4366-74
pubmed: 9780214
J Mol Biol. 1998 Aug 21;281(3):523-37
pubmed: 9698567
Immunol Rev. 2009 Nov;232(1):286-99
pubmed: 19909371
J Biol Chem. 2008 Nov 21;283(47):32650-9
pubmed: 18818202
J Biol Chem. 2000 Nov 10;275(45):35442-7
pubmed: 10931839
Eur J Biochem. 1997 Jun 1;246(2):447-51
pubmed: 9208937
Structure. 1995 Oct 15;3(10):1061-73
pubmed: 8590001
Biochim Biophys Acta. 2009 Aug;1794(8):1211-7
pubmed: 19409513
J Mol Biol. 2013 Jan 23;425(2):309-33
pubmed: 23154170
Nat Rev Immunol. 2010 Jun;10(6):387-402
pubmed: 20467426
Proc Natl Acad Sci U S A. 2008 Aug 19;105(33):11760-5
pubmed: 18689684
Mol Immunol. 2010 Nov-Dec;48(1-3):171-8
pubmed: 20828828
Cold Spring Harb Perspect Biol. 2011 Mar 01;3(3):
pubmed: 21068150
Biochim Biophys Acta. 1997 Feb 4;1355(2):177-90
pubmed: 9042338
J Biol Chem. 2004 Mar 12;279(11):10176-84
pubmed: 14688255
Eur J Immunol. 2011 Jun;41(6):1550-62
pubmed: 21469132
Expert Opin Ther Pat. 2014 May;24(5):573-95
pubmed: 24555683