RalGDS family members couple Ras to Ral signalling and that's not all.

Abstract:

:Ras proteins function as molecular switches that are activated in response to signalling pathways initiated by various extracellular stimuli and subsequently bind to numerous effector proteins leading to the activation of several signalling cascades within the cell. Ras and Ras-related proteins belong to a large superfamily of small GTPases characterized by significant sequence and function similarities. Several evidence indicate the existence of complex signalling networks that link Ras with its relatives in the family. A key role in this cross-talk is played by guanine nucleotide exchange factors (GEFs) that serve both as regulators and as effectors of Ras family proteins. The members of the RalGDS family, RalGDS, RGL, RGL2/Rlf and RGL3, can interact with activated Ras through their Ras Binding Domain (RBD), but may function as effectors for other Ras family members. They possess a REM-CDC25 homology region like RasGEFs, but specifically activate only RalA and RalB and not Ras or other Ras-related small GTPases. In this review we provide an update on this recently discovered family of GEFs, highlighting their crucial role in coupling activated Ras to activation of Ral, thus regulating several fundamental cell processes, and also discussing some evidence supporting Ras-independent additional functions of RalGDS proteins.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Ferro E,Trabalzini L

doi

10.1016/j.cellsig.2010.05.010

subject

Has Abstract

pub_date

2010-12-01 00:00:00

pages

1804-10

issue

12

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(10)00140-3

journal_volume

22

pub_type

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