Abstract:
:The protein tyrosine kinase Syk couples the B-cell receptor (BCR) for antigen to multiple intracellular signaling pathways and also modulates cellular responses to inducers of oxidative stress in a receptor-independent fashion. In B cells, Syk is found in both the nuclear and cytoplasmic compartments but contains no recognizable nuclear localization or export signals. Through the analysis of a series of deletion mutants, we identified the presence of an unconventional shuttling sequence near the junction of the catalytic domain and the linker B region that accounts for Syk's subcellular localization. This localization is altered following prolonged engagement of the BCR, which causes Syk to be excluded from the nucleus. Nuclear exclusion requires the receptor-mediated activation of protein kinase C and new protein synthesis. Both of these processes also potentiate the activation of caspase 3 in cells in response to oxidative stress in a manner that is dependent on the localization of Syk outside of the nucleus. In contrast, restriction of Syk to the nucleus greatly diminishes the stress-induced activation of caspase 3.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Zhou F,Hu J,Ma H,Harrison ML,Geahlen RLdoi
10.1128/MCB.26.9.3478-3491.2006subject
Has Abstractpub_date
2006-05-01 00:00:00pages
3478-91issue
9eissn
0270-7306issn
1098-5549pii
26/9/3478journal_volume
26pub_type
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