Nucleocytoplasmic Trafficking of the Syk Protein Tyrosine Kinase
نویسندگان
چکیده
منابع مشابه
Phosphorylation of Staphylococcus aureus Protein-Tyrosine Kinase Affects the Function of Glucokinase and Biofilm Formation
Background: When Staphylococcus aureus is grown in the presence of high concentration of external glucose, this sugar is phosphorylated by glucokinase (glkA) to form glucose-6-phosphate. This product subsequently enters into anabolic phase, which favors biofilm formation. The presence of ROK (repressor protein, open reading frame, sugar kinase) motif, phosphate-1 and -2 sites, and tyrosine kina...
متن کاملMolecular basis for a direct interaction between the Syk protein-tyrosine kinase and phosphoinositide 3-kinase.
After engagement of the B cell receptor for antigen, the Syk protein-tyrosine kinase becomes phosphorylated on multiple tyrosines, some of which serve as docking sites for downstream effectors with SH2 or other phosphotyrosine binding domains. The most frequently identified binding partner for catalytically active Syk identified in a yeast two-hybrid screen was the p85 regulatory subunit of pho...
متن کاملNucleocytoplasmic trafficking
Nucleocytoplasmic trafficking describes the process whereby molecules destined for the nucleoplasm or cytoplasm move across the nuclear envelope. This transport regulates transcription and translation by respective control of transnuclear movements of transcription factors and messenger RNA. Transport across the nuclear envelope occurs through large MDa pores embedded in the inner and outer nuc...
متن کاملSyk inhibits the activity of protein kinase A by phosphorylating tyrosine 330 of the catalytic subunit.
The Syk protein-tyrosine kinase can have multiple effects on cancer cells, acting in some as a tumor suppressor by inhibiting motility and in others as a tumor promoter by enhancing survival. Phosphoproteomic analyses identified PKA as a Syk-specific substrate. Syk catalyzes the phosphorylation of the catalytic subunit of PKA (PKAc) both in vitro and in cells on Tyr-330. Tyr-330 lies within the...
متن کاملRedundant role of the Syk protein tyrosine kinase in mouse NK cell differentiation.
Syk and ZAP-70 subserve nonredundant functions in B and T lymphopoiesis. In the absence of Syk, B cell development is blocked, while T cell development is arrested in the absence of ZAP-70. The receptors and the signaling molecules required for differentiation of NK cells are poorly characterized. Here we investigate the role of the Syk protein tyrosine kinase in NK cell differentiation. Hemopo...
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ژورنال
عنوان ژورنال: Molecular and Cellular Biology
سال: 2006
ISSN: 0270-7306,1098-5549
DOI: 10.1128/mcb.26.9.3478-3491.2006