RanGAP is a protein involved in the transport of other proteins from the cytosol to the nucleus in eukaryotic cells. In model species such as the yeast Saccharomyces cerevisiae, the primate Homo sapiens (See RANGAP1) and the plant Arabidopsis thaliana, it acts as a GTPase-activating protein, catalysing the conversion of cytosolically-bound ...

RanGAP1, is a homodimeric 65-kD polypeptide that specifically induces the GTPase activity of RAN, but not of RAS by over 1,000-fold. RanGAP1 is the immediate antagonist of RCC1, a regulator molecule that keeps RAN in the active, GTP -bound state. The RANGAP1 gene encodes a 587-amino acid polypeptide.

RanGAPs are members of a family of proteins that harbor a characteristic array of leucine-rich repeats. Budding yeast rna1p includes 11 such repeats and adopts a crescent-like shape containing both alpha helices and beta sheets that is unlike any other GAP structure [76].

Mar 30, 2025 · RANGAP1 (Ran GTPase Activating Protein 1) is a Protein Coding gene. Diseases associated with RANGAP1 include Nephronophthisis-Like Nephropathy 1 and Parkinson Disease 7, Autosomal Recessive Early-Onset. Among its related pathways are EML4 and NUDC in mitotic spindle formation and Transport of the SLBP independent Mature mRNA.

We propose that Arabidopsis RanGAP, a continuous positive protein marker of the plant division plane, has a role in spatial signaling during plant cell division. Keywords: cytokinesis, Ran cycle, preprophase band, nuclear pore.

May 10, 2016 · Here, we show that the RanBP2/RanGAP1*SUMO1/Ubc9 complex functions as an autonomous disassembly machine with a preference for the export receptor Crm1.

In mammalian cells, unmodified RanGAP1 is predominantly cytoplasmic, whereas modification by small ubiquitin-related modifier protein (SUMO) targets RanGAP1 to the cytoplasmic filaments of nuclear pore complex (NPC).

Ran’s GTPase activating protein (RanGAP) is tethered to the nuclear envelope (NE) in multicellular organisms. We investigated the consequences of RanGAP localization in human tissue culture cells and Drosophila.

In vertebrate cells, the nucleoporin Nup358/RanBP2 is a major component of the filaments that emanate from the nuclear pore complex into the cytoplasm. Nup358 forms a complex with SUMOylated RanGAP1, the GTPase activating protein for Ran.

Localization of RanGAP (A and C) or chromatin (B and D) in either Saccharomyces cerevisiae wild-type (A and B) or rangapΔC362 (C and D) cells. RanGAP staining was performed using primary anti-RanGAP antibodies and secondary fluorescein isothiocyanate-labeled antibodies.