Abstract:
:The Epstein-Barr virus latency-associated membrane protein LMP2A has been shown to activate the survival kinase Akt in epithelial and B cells in a phosphoinositide 3-kinase-dependent fashion. In this study, we demonstrate that the signalling scaffold Shb associates through SH2 and PTB domain interactions with phosphorylated tyrosine motifs in the LMP2A N-terminal tail. Additionally, we show that mutation of tyrosines in these motifs as well as shRNA-mediated downregulation of Shb leads to a loss of constitutive Akt-activation in LMP2A-expressing cells. Furthermore, utilization by Shb of the LMP2A ITAM motif regulates stability of the Syk tyrosine kinase in LMP2A-expressing cells. Our data set the precedent for viral utilization of the Shb signalling scaffold and implicate Shb as a regulator of LMP2A-dependent Akt activation.
journal_name
Oncogenejournal_title
Oncogeneauthors
Matskova LV,Helmstetter C,Ingham RJ,Gish G,Lindholm CK,Ernberg I,Pawson T,Winberg Gdoi
10.1038/sj.onc.1210298subject
Has Abstractpub_date
2007-07-26 00:00:00pages
4908-17issue
34eissn
0950-9232issn
1476-5594pii
1210298journal_volume
26pub_type
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