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Article

The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, RAN-GAP, and HTF9A/RANBP1.

The Journal of biological chemistry - 16 Jun 1995

Richards S A, Lounsbury K M, Macara I G

Abstract excerpt

Ran/TC4 is a member of the Ras superfamily of GTPases. It is unusual in being predominantly nuclear and because it possesses an acidic -DEDDDL sequence instead of a consensus prenylation domain at the C terminus. Ran is required for nuclear protein import and cell cycle progression, and has been implicated in mRNA processing and export and DNA replication. The inhibition of cell cycle progression by a dominant...

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Source

Identifiers

PMID: 7782302
DOI: 10.1074/jbc.270.24.14405

Genes

RAN
RANBP1
RCC1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, RAN-GAP, and HTF9A/RANBP1.PMID 7782302Read ↗

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Destabilization of Ran C-terminus promotes GTP loading and occurs in multiple Ran cancer mutationsSemantic proximity Read ↗

A T42A Ran mutation: differential interactions with effectors and regulators, and defect in nuclear protein import.Semantic proximity Read ↗

RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits RCC1 via Ran/TC4.Semantic proximity Read ↗

A mutant form of the Ran/TC4 protein disrupts nuclear function in Xenopus laevis egg extracts by inhibiting the RCC1 protein, a regulator of chromosome condensation.Semantic proximity Read ↗

Ran GTPase and Its Importance in Cellular Signaling and Malignant Phenotype.Semantic proximity Read ↗

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