scholarly journals Zinc clasp-based reversible toolset for selective metal-mediated protein heterodimerization

2018 ◽  
Vol 54 (96) ◽  
pp. 13539-13542 ◽  
Author(s):  
Anna Kocyła ◽  
Artur Krężel
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
High Specificity ◽  
Stable Complex ◽  
Kinetic Properties ◽  
Protein Tyrosine ◽  
Peptide Tags ◽  
Lck Protein

Zinc clasp motif derived from natural Zn(ii)-mediated interaction of CD4 co-receptor and Lck protein tyrosine kinase was used for specific and efficient protein heterodimerization. Optimized set of peptide tags forms highly stable complex in the selective heterodimer framework. Utility of obtained toolset demonstrates high specificity, Zn(ii)-dependent reversibility and remarkable kinetic properties.

scholarly journals ZAP-70 Protein Tyrosine Kinase Is Constitutively Targeted to the T Cell Cortex Independently of its SH2 Domains

1997 ◽  
Vol 137 (7) ◽  
pp. 1639-1649 ◽  
Author(s):  
Russell D.J. Huby ◽  
Makio Iwashima ◽  
Arthur Weiss ◽  
Steven C. Ley
Keyword(s):  
T Cell ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Kinase Domain ◽  
Cell Cortex ◽  
Protein Tyrosine ◽  
Sh2 Domains ◽  
Anchoring Protein ◽  
High Concentrations ◽  
Lck Protein

ZAP-70 is a nonreceptor protein tyrosine kinase that is essential for signaling via the T cell antigen receptor (TCR). ZAP-70 becomes phosphorylated and activated by LCK protein tyrosine kinase after interaction of its two NH2-terminal SH2 domains with tyrosine-phosphorylated subunits of the activated TCR. In this study, the localization of ZAP-70 was investigated by immunofluorescence and confocal microscopy. ZAP-70 was found to be localized to the cell cortex in a diffuse band under the plasma membrane in unstimulated T cells, and this localization was not detectably altered by TCR stimulation. Analysis of mutants indicated that ZAP-70 targeting was independent of its SH2 domains but required its active kinase domain. The specific compartmentalization of ZAP-70 suggests that it may interact with an anchoring protein in the cell cortex via its hinge or kinase domains. It is likely that the maintenance of high concentrations of ZAP-70 at the cell cortex, that only has to move a short distance to interact with phophorylated TCR subunits, facilitates rapid initiation of signaling by the TCR. In addition, as the major increase in tyrosine phosphorylation induced by the TCR also occurs at the cell cortex (Ley, S.C., M. Marsh, C.R. Bebbington, K. Proudfoot, and P. Jordan. 1994. J. Cell. Biol. 125:639–649), ZAP-70 may be localized close to its downstream targets.

scholarly journals The lck protein tyrosine kinase is not involved in antibody-mediated CD4 (CDR3-loop) signal transduction that inhibits HIV-1 transcription

1998 ◽  
Vol 28 (5) ◽  
pp. 1445-1457 ◽  
Author(s):  
Nolwenn Coudronnière ◽  
Jacques Corbeil ◽  
Véronique Robert-Hebmann ◽  
Jean-Michel Mesnard ◽  
Christian Devaux
Keyword(s):  
Signal Transduction ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine ◽  
Lck Protein ◽  
Hiv 1

scholarly journals Tyr394 and Tyr505 are Autophosphorylated in Recombinant Lck Protein-tyrosine Kinase Expressed in Escherichia coli

1994 ◽  
Vol 224 (2) ◽  
pp. 589-596 ◽  
Author(s):  
Pascale Jullien ◽  
Cecile Bougeret ◽  
Luc Camoin ◽  
Monique Bodeus ◽  
Herve Durand ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Protein Tyrosine ◽  
Lck Protein

Protein-tyrosine Kinase p72 syk Is Activated by Platelet Activating Factor in Platelets

1994 ◽  
Vol 72 (06) ◽  
pp. 937-941 ◽  
Author(s):  
Karim Rezaul ◽  
Shigeru Yanagi ◽  
Kiyonao Sada ◽  
Takanobu Taniguchi ◽  
Hirohei Yamamura
Keyword(s):  
Tyrosine Kinase ◽  
Tyrosine Phosphorylation ◽  
Protein Tyrosine Kinase ◽  
Kinase Inhibitor ◽  
Critical Role ◽  
Platelet Activating Factor ◽  
Kinase Assay ◽  
Potential Candidate ◽  
Protein Tyrosine ◽  
Induced Aggregation

SummaryIt has been demonstrated that activation of platelets by platelet-activating factor (PAF) results in a dramatic increase in tyrosine phosphorylation of several cellular proteins. We report here that p72 syk is a potential candidate for the protein-tyrosine phosphorylation following PAF stimulation in porcine platelets. Immunoprecipitation kinase assay revealed that PAF stimulation resulted in a rapid activation of p72 syk which peaked at 10 s. The level of activation was found to be dose dependent and could be completely inhibited by the PAF receptor antagonist, CV3988. Phosphorylation at the tyrosine residues of p72 syk coincided with activation of yllsyk. Pretreatment of platelets with aspirin and apyrase did not affect PAF induced activation of p72 syk .Furthermore, genistein, a potent protein-tyrosine-kinase inhibitor, diminished PAF-induced p72 syk activation and Ca2+ mobilization as well as platelet aggregation. These results suggest that p72 syk may play a critical role in PAF-induced aggregation, possibly through regulation of Ca2+ mobilization.

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