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TitleThe GTPase κB-Ras is an essential subunit of the RalGAP tumor suppressor complex.
Journal, issue, pagesJ Biol Chem, Vol. 301, Issue 8, Page 110460, Year 2025
Publish dateJul 5, 2025
AuthorsRené Rasche / Lisa Helene Apken / Sonja Titze / Esther Michalke / Rohit Kumar Singh / Andrea Oeckinghaus / Daniel Kümmel /
PubMed AbstractκB-Ras1 and κB-Ras2 are small GTPases with noncanonical features that act as tumor suppressors downstream of Ras. Via interaction with the RalGAP (GTPase-activating protein) complex, they limit ...κB-Ras1 and κB-Ras2 are small GTPases with noncanonical features that act as tumor suppressors downstream of Ras. Via interaction with the RalGAP (GTPase-activating protein) complex, they limit activity of Ral GTPases and restrict anchorage-independent proliferation. We here present the crystal structure of κB-Ras1 in complex with the N-terminal domain of RGα2. The structure suggests a mechanism of intrinsic GTP hydrolysis of κB-Ras1 that relies on a scaffolding function of the GTPase rather than on catalytic residues, which we confirm by mutational analysis. The interaction with RGα2 is nucleotide independent and does not involve κB-Ras1 switch regions, which establishes κB-Ras proteins as a constitutive third subunit of RalGAP complexes. Functional studies demonstrate that κB-Ras proteins are not required for RalGAP catalytic activity in vitro but for functionality in vivo. We propose that κB-Ras may thus act as a regulator of RalGAP localization and thereby control the Ras-Ral signaling pathway.
External linksJ Biol Chem / PubMed:40619001 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.72 - 4.35 Å
Structure data

EMDB-53418: Consensus cryo EM map of the human RalGAP2 complex
Method: EM (single particle) / Resolution: 3.83 Å

EMDB-53419: Focussed cryo EM map from multibody refinement of human RalGAP2 complex (body1: alpha2 beta heterodimer interface)
Method: EM (single particle) / Resolution: 3.79 Å

EMDB-53420: Focussed cryo EM map from multibody refinement of human RalGAP2 complex (body2: alpha2 N-terminus)
Method: EM (single particle) / Resolution: 3.93 Å

EMDB-53421: Focussed cryo EM map from multibody refinement of human RalGAP2 complex (body3: beta-beta homodimer interface)
Method: EM (single particle) / Resolution: 4.35 Å

53422

9qwp

EMDB-53422, PDB-9qwp:
Structure of the human RalGAP2 complex
Method: EM (single particle) / Resolution: 3.8 Å

PDB-9qu1:
Crystal structure of the human RalGAPA2 N-terminal domain with human kappaB-Ras1
Method: X-RAY DIFFRACTION / Resolution: 2.72 Å

Chemicals

ChemComp-GNP:
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GppNHp, GMPPNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / RAL / GTPase / RalGAP / kB-Ras / Complex / GTPase activating protein / Asn thumb GAP

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