Shuttling and translocation of heterotrimeric G proteins and Ras

Deepak K. Saini, Mariangela Chisari, N. Gautam

Research output: Contribution to journalReview articlepeer-review

40 Scopus citations

Abstract

Heterotrimeric G proteins (αβγ) and Ras proteins are activated by cell-surface receptors that sense extracellular signals. Both sets of proteins were traditionally thought to be constrained to the plasma membrane and some intracellular membranes. Live-cell-imaging experiments have now shown that these proteins are mobile inside a cell, shuttling continually between the plasma membrane and intracellular membranes in the basal state, maintaining these proteins in dynamic equilibrium in different membrane compartments. Furthermore, on receptor activation, a family of G protein βγ subunits translocates rapidly and reversibly to the Golgi and endoplasmic reticulum enabling direct communication between the extracellular signal and intracellular membranes. A member of the Ras family has similarly been shown to translocate on activation. Although the impact of this unexpected intracellular movement of signaling proteins on cell physiology is likely to be distinct, there are striking similarities in the properties of these two families of signal-transducing proteins.

Original languageEnglish
Pages (from-to)278-286
Number of pages9
JournalTrends in Pharmacological Sciences
Volume30
Issue number6
DOIs
StatePublished - Jun 2009

Fingerprint

Dive into the research topics of 'Shuttling and translocation of heterotrimeric G proteins and Ras'. Together they form a unique fingerprint.

Cite this