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The pleckstrin homology domain of Gab-2 is required for optimal interleukin-3 signalsome-mediated responses.

Abstract：

:The adaptor protein Gab-2 coordinates the assembly of the IL-3 signalsome comprising Gab-2, Grb2, Shc, SHP-2 and PI3K. To investigate the role of the pleckstrin homology domain of Gab-2 in this process, epitope-tagged wild type Gab-2 (WTGab-2), Gab-2 lacking its PH domain (DeltaPHGab-2) and the Gab-2 PH domain alone (PHGab-2) were inducibly expressed in IL-3-dependent BaF/3 cells. Expression of DeltaPHGab-2 reduced IL-3-dependent proliferation and long-term activation of ERK1 and 2 and PKB by IL-3. While we demonstrate that the Gab-2 PH domain can bind PI(3,4,5)P3, it is dispensable for Gab-2 membrane localisation, tyrosine phosphorylation and signalsome formation. Rather, the proline-rich motifs of Gab-2 appear to contribute to the constitutive membrane localisation we observe, independently of tyrosine phosphorylation or the PH domain. Taken together, these findings suggest that once Gab-2 is tyrosine phosphorylated its PH domain is required for the optimal stabilisation of the signalsome, enabling full activation of downstream signals.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Edmead CE,Fox BC,Stace C,Ktistakis N,Welham MJ

doi

10.1016/j.cellsig.2005.09.002

subject

Has Abstract

pub_date

2006-08-01 00:00:00

pages

1147-55

issue

8

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(05)00241-X

journal_volume

18

pub_type

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